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Journal articles on the topic 'Aldehyde oxidoreductase'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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1

Bevers, Loes E., Emile Bol, Peter-Leon Hagedoorn, and Wilfred R. Hagen. "WOR5, a Novel Tungsten-Containing Aldehyde Oxidoreductase from Pyrococcus furiosus with a Broad Substrate Specificity." Journal of Bacteriology 187, no. 20 (October 15, 2005): 7056–61. http://dx.doi.org/10.1128/jb.187.20.7056-7061.2005.

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ABSTRACT WOR5 is the fifth and last member of the family of tungsten-containing oxidoreductases purified from the hyperthermophilic archaeon Pyrococcus furiosus. It is a homodimeric protein (subunit, 65 kDa) that contains one [4Fe-4S] cluster and one tungstobispterin cofactor per subunit. It has a broad substrate specificity with a high affinity for several substituted and nonsubstituted aliphatic and aromatic aldehydes with various chain lengths. The highest catalytic efficiency of WOR5 is found for the oxidation of hexanal (V max = 15.6 U/mg, Km = 0.18 mM at 60°C). Hexanal-incubated enzyme exhibits S = 1/2 electron paramagnetic resonance signals from [4Fe-4S]1+ (g values of 2.08, 1.93, and 1.87) and W5+ (g values of 1.977, 1.906, and 1.855). Cyclic voltammetry of ferredoxin and WOR5 on an activated glassy carbon electrode shows a catalytic wave upon addition of hexanal, suggesting that ferredoxin can be a physiological redox partner. The combination of WOR5, formaldehyde oxidoreductase, and aldehyde oxidoreductase forms an efficient catalyst for the oxidation of a broad range of aldehydes in P. furiosus.

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2

GARATTINI, Enrico, Ralf MENDEL, Maria João ROMÃO, Richard WRIGHT, and Mineko TERAO. "Mammalian molybdo-flavoenzymes, an expanding family of proteins: structure, genetics, regulation, function and pathophysiology." Biochemical Journal 372, no. 1 (May 15, 2003): 15–32. http://dx.doi.org/10.1042/bj20030121.

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The molybdo–flavoenzymes are structurally related proteins that require a molybdopterin cofactor and FAD for their catalytic activity. In mammals, four enzymes are known: xanthine oxidoreductase, aldehyde oxidase and two recently described mouse proteins known as aldehyde oxidase homologue 1 and aldehyde oxidase homologue 2. The present review article summarizes current knowledge on the structure, enzymology, genetics, regulation and pathophysiology of mammalian molybdo–flavoenzymes. Molybdo–flavoenzymes are structurally complex oxidoreductases with an equally complex mechanism of catalysis. Our knowledge has greatly increased due to the recent crystallization of two xanthine oxidoreductases and the determination of the amino acid sequences of many members of the family. The evolution of molybdo–flavoenzymes can now be traced, given the availability of the structures of the corresponding genes in many organisms. The genes coding for molybdo–flavoenzymes are expressed in a cell-specific fashion and are controlled by endogenous and exogenous stimuli. The recent cloning of the genes involved in the biosynthesis of the molybdenum cofactor has increased our knowledge on the assembly of the apo-forms of molybdo–flavoproteins into the corresponding holo-forms. Xanthine oxidoreductase is the key enzyme in the catabolism of purines, although recent data suggest that the physiological function of this enzyme is more complex than previously assumed. The enzyme has been implicated in such diverse pathological situations as organ ischaemia, inflammation and infection. At present, very little is known about the pathophysiological relevance of aldehyde oxidase, aldehyde oxidase homologue 1 and aldehyde oxidase homologue 2, which do not as yet have an accepted endogenous substrate.

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3

Chen, Jun, and Shulin Yang. "Catalytic mechanism of UDP-glucose dehydrogenase." Biochemical Society Transactions 47, no. 3 (June 12, 2019): 945–55. http://dx.doi.org/10.1042/bst20190257.

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AbstractUDP-glucose dehydrogenase (UGDH), an oxidoreductase, catalyzes the NAD+-dependent four-electron oxidation of UDP-glucose to UDP-glucuronic acid. The catalytic mechanism of UGDH remains controversial despite extensive investigation and is classified into two types according to whether an aldehyde intermediate is generated in the first oxidation step. The first type, which involves the presence of this putative aldehyde, is inconsistent with some experimental findings. In contrast, the second type, which indicates that the first oxidation step bypasses the aldehyde via an NAD+-dependent bimolecular nucleophilic substitution (SN2) reaction, is consistent with the experimental phenomena, including those that cannot be explained by the first type. This NAD+-dependent SN2 mechanism is thus more reasonable and likely applicable to other oxidoreductases that catalyze four-electron oxidation reactions.

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4

Rauh, David, Andrea Graentzdoerffer, Katrin Granderath, Jan R. Andreesen, and Andreas Pich. "Tungsten-containing aldehyde oxidoreductase of Eubacterium acidaminophilum." European Journal of Biochemistry 271, no. 1 (December 19, 2003): 212–19. http://dx.doi.org/10.1111/j.1432-1033.2004.03922.x.

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5

Badalyan, Artavazd, Meina Neumann-Schaal, Silke Leimkühler, and Ulla Wollenberger. "A Biosensor for Aromatic Aldehydes Comprising the Mediator Dependent PaoABC-Aldehyde Oxidoreductase." Electroanalysis 25, no. 1 (October 10, 2012): 101–8. http://dx.doi.org/10.1002/elan.201200362.

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6

Correia dos Santos, Margarida M., Patrícia M. P. Sousa, M. Lurdes S. Gonçalves, M. João Romão, Isabel Moura, and José J. G. Moura. "Direct electrochemistry of the Desulfovibrio gigas aldehyde oxidoreductase." European Journal of Biochemistry 271, no. 7 (March 23, 2004): 1329–38. http://dx.doi.org/10.1111/j.1432-1033.2004.04041.x.

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7

Andrade, Susana L. A., Carlos D. Brondino, Maria J. Feio, Isabel Moura, and José J. G. Moura. "Aldehyde oxidoreductase activity in Desulfovibrio alaskensis NCIMB 13491." European Journal of Biochemistry 267, no. 7 (April 2000): 2054–61. http://dx.doi.org/10.1046/j.1432-1327.2000.01209.x.

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8

Rivas, Maria Gabriela, Pablo Javier Gonzalez, Felix Martin Ferroni, Alberto Claudio Rizzi, and Carlos Brondino. "Studying Electron Transfer Pathways in Oxidoreductases." Science Reviews - from the end of the world 1, no. 2 (March 16, 2020): 6–23. http://dx.doi.org/10.52712/sciencereviews.v1i2.15.

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Oxidoreductases containing transition metal ions are widespread in nature and are essential for living organisms. The copper-containing nitrite reductase (NirK) and the molybdenum-containing aldehyde oxidoreductase (Aor) are typical examples of oxidoreductases. Metal ions in these enzymes are present either as mononuclear centers or organized into clusters and accomplish two main roles. One of them is to be the active site where the substrate is converted into product, and the other one is to serve as electron transfer center. Both enzymes transiently bind the substrate and an external electron donor/acceptor in NirK/Aor, respectively, at distinct protein points for them to exchange the electrons involved in the redox reaction. Electron exchange occurs through a specific intra-protein chemical pathway that connects the different enzyme metal cofactors. Based on the two oxidoreductases presented here, we describe how the different actors involved in the intra-protein electron transfer process can be characterized and studied employing molecular biology, spectroscopic, electrochemical, and structural techniques.

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9

Golwala, Neel H., Christopher Hodenette, Subramanyam N. Murthy, Bobby D. Nossaman, and Philip J. Kadowitz. "Vascular responses to nitrite are mediated by xanthine oxidoreductase and mitochondrial aldehyde dehydrogenase in the ratThis article is one of a selection of papers published in a special issue on Advances in Cardiovascular Research." Canadian Journal of Physiology and Pharmacology 87, no. 12 (December 2009): 1095–101. http://dx.doi.org/10.1139/y09-101.

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Sodium nitrite has been shown to have vasodilator activity in experimental animals and in human subjects. However, the mechanism by which nitrite anion is converted to vasoactive nitric oxide (NO) is uncertain. It has been hypothesized that deoxyhemoglobin, xanthine oxidoreductase, mitochondrial aldehyde dehydrogenase, and other heme proteins can reduce nitrite to NO, but studies in the literature have not identified the mechanism in the intact rat, and several studies report no effect of inhibitors of xanthine oxidoreductase. In the present study, the effects of the xanthine oxidoreductase inhibitor allopurinol and the mitochondrial aldehyde dehydrogenase inhibitor cyanamide on decreases in mean systemic arterial pressure in response to i.v. sodium nitrite administration were investigated in the rat. The decreases in mean systemic arterial pressure in response to i.v. administration of sodium nitrite were inhibited in a selective manner after administration of allopurinol in a dose of 25 mg/kg i.v. A second 25 mg/kg i.v. dose had no additional inhibitory effect on the response to sodium nitrite. The decreases in mean systemic arterial pressure in response to sodium nitrite were attenuated by cyanamide and a second 25 mg/kg i.v. dose had no additional inhibitory effect. In l-NAME-treated animals, allopurinol attenuated responses to sodium nitrite and a subsequent administration of cyanamide had no additional effect. When the order of administration of the inhibitors was reversed, responses to sodium nitrite were attenuated by administration of cyanamide and a subsequent administration of allopurinol had no additional inhibitory effect. The results of these studies suggest that nitrite can be reduced to vasoactive NO in the systemic vascular bed of the rat by xanthine oxidoreductase and mitochondrial aldehyde dehydrogenase and that the 2 pathways of nitrite activation act in a parallel manner.

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10

Chan, M., S. Mukund, A. Kletzin, M. Adams, and D. Rees. "Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase." Science 267, no. 5203 (March 10, 1995): 1463–69. http://dx.doi.org/10.1126/science.7878465.

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11

Venkitasubramanian, Padmesh, Lacy Daniels, Shuvendu Das, Andrew S. Lamm, and John P. N. Rosazza. "Aldehyde oxidoreductase as a biocatalyst: Reductions of vanillic acid." Enzyme and Microbial Technology 42, no. 2 (January 2008): 130–37. http://dx.doi.org/10.1016/j.enzmictec.2007.08.009.

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12

STROBL, Gerhard, Richard FEICHT, Hiltrud WHITE, Friedrich LOTTSPEICH, and Helmut SIMON. "The Tungsten-Containing Aldehyde Oxidoreductase fromClostridium thermoaceticumand its Complex with a Viologen-Accepting NADPH Oxidoreductase." Biological Chemistry Hoppe-Seyler 373, no. 1 (January 1992): 123–32. http://dx.doi.org/10.1515/bchm3.1992.373.1.123.

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13

Sevcenco, Ana-Maria, Loes E. Bevers, Martijn W. H. Pinkse, Gerard C. Krijger, Hubert T. Wolterbeek, Peter D. E. M. Verhaert, Wilfred R. Hagen, and Peter-Leon Hagedoorn. "Molybdenum Incorporation in Tungsten Aldehyde Oxidoreductase Enzymes from Pyrococcus furiosus." Journal of Bacteriology 192, no. 16 (June 18, 2010): 4143–52. http://dx.doi.org/10.1128/jb.00270-10.

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ABSTRACT The hyperthermophilic archaeon Pyrococcus furiosus expresses five aldehyde oxidoreductase (AOR) enzymes, all containing a tungsto-bispterin cofactor. The growth of this organism is fully dependent on the presence of tungsten in the growth medium. Previous studies have suggested that molybdenum is not incorporated in the active site of these enzymes. Application of the radioisotope 99Mo in metal isotope native radioautography in gel electrophoresis (MIRAGE) technology to P. furiosus shows that molybdenum can in fact be incorporated in all five AOR enzymes. Mo(V) signals characteristic for molybdopterin were observed in formaldehyde oxidoreductase (FOR) in electron paramagnetic resonance (EPR)-monitored redox titrations. Our finding that the aldehyde oxidation activity of FOR and WOR5 (W-containing oxidoreductase 5) correlates only with the residual tungsten content suggests that the Mo-containing AORs are most likely inactive. An observed W/Mo antagonism is indicative of tungstate-dependent negative feedback of the expression of the tungstate/molybdate ABC transporter. An intracellular selection mechanism for tungstate and molybdate processing has to be present, since tungsten was found to be preferentially incorporated into the AORs even under conditions with comparable intracellular concentrations of tungstate and molybdate. Under the employed growth conditions of starch as the main carbon source in a rich medium, no tungsten- and/or molybdenum-associated proteins are detected in P. furiosus other than the high-affinity transporter, the proteins of the metallopterin insertion machinery, and the five W-AORs.

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14

Krippahl, Ludwig, P. Nuno Palma, Isabel Moura, and José J. G. Moura. "Modelling the Electron-Transfer Complex Between Aldehyde Oxidoreductase and Flavodoxin." European Journal of Inorganic Chemistry 2006, no. 19 (October 2006): 3835–40. http://dx.doi.org/10.1002/ejic.200600418.

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15

White, Hiltrud, Claudia Huber, Richard Feicht, and Helmut Simon. "On a reversible molybdenum-containing aldehyde oxidoreductase from Clostridium formicoaceticum." Archives of Microbiology 159, no. 3 (March 1993): 244–49. http://dx.doi.org/10.1007/bf00248479.

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16

SRIVASTAVA, Sanjay, Animesh CHANDRA, H. Naseem ANSARI, K. Satish SRIVASTAVA, and Aruni BHATNAGAR. "Identification of cardiac oxidoreductase(s) involved in the metabolism of the lipid peroxidation-derived aldehyde-4-hydroxynonenal." Biochemical Journal 329, no. 3 (February 1, 1998): 469–75. http://dx.doi.org/10.1042/bj3290469.

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The aim of this study was to identify the cardiac oxidoreductases involved in the metabolism of 4-hydroxy-2-trans-nonenal (HNE), an α,β unsaturated aldehyde generated during the peroxidation of ω-6 polyunsaturated fatty acids. In homogenates of bovine, human and rat ventricles the primary pyridine coenzyme-linked metabolism of HNE was associated with NADPH oxidation. The NADPH-dependent enzyme catalysing HNE reduction was purified to homogeneity from bovine heart. The purified enzyme displayed kinetic and immunological properties identical with the polyol pathway enzyme aldose reductase (AR), and catalysed the reduction of HNE to its alcohol 1,4-dihydroxynonene (DHN), with a Km of 7±2 μM. In the presence of NADP the enzyme did not catalyse the oxidation of DHN. During catalysis, HNE did not cause inactivation of AR. Nevertheless when the apoenzyme was incubated with HNE a dissociable complex was formed between the enzyme and HNE, followed by irreversible loss of activity. Inactivation of the enzyme by HNE was prevented by NADP. Partial modification of the enzyme with HNE led to a 17-fold increase in the KHNEm and Kglyceraldehydem, and the HNE-modified enzyme had a 500-fold higher IC50 for sorbinil than for the reduced enzyme, whereas the IC50 for tolrestat increased 25-fold. Incubation of the enzyme with radiolabelled HNE resulted in the incorporation of 2 mol of the aldehyde per mol of the enzyme. Sequence analysis of the radiolabelled peptides revealed modification of Cys-298 and Cys-187. The amino acid sequence of the HNE-modified peptides confirmed that the HNE-reducing cardiac enzyme is AR and not a related protein such as the fibroblast-growth-factor-regulated protein FR-1 or the mouse vas deferens protein MVDP. These results indicate that AR represents the only major oxidoreductase in the heart capable of utilizing HNE. The high affinity of the enzyme for HNE, the lack of inactivation during catalysis, and the lack of significant alcohol dehydrogenase activity of the protein suggests that AR-mediated catalysis of HNE is unlikely to be limited by substrate/product inhibition. Thus AR might constitute an antioxidative enzyme involved in myocardial protection against endogenous and exogenous cytotoxic aldehydes and against oxidative stress.

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17

Andrade, Susana L. A., Carlos D. Brondino, Elvira O. Kamenskaya, Andrey V. Levashov, and José J. G. Moura. "Kinetic behavior of Desulfovibrio gigas aldehyde oxidoreductase encapsulated in reverse micelles." Biochemical and Biophysical Research Communications 308, no. 1 (August 2003): 73–78. http://dx.doi.org/10.1016/s0006-291x(03)01337-8.

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18

Verma, Rajni, Jonathan M. Ellis, and Katie R. Mitchell-Koch. "Dynamic Preference for NADP/H Cofactor Binding/Release in E. coli YqhD Oxidoreductase." Molecules 26, no. 2 (January 7, 2021): 270. http://dx.doi.org/10.3390/molecules26020270.

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YqhD, an E. coli alcohol/aldehyde oxidoreductase, is an enzyme able to produce valuable bio-renewable fuels and fine chemicals from a broad range of starting materials. Herein, we report the first computational solution-phase structure-dynamics analysis of YqhD, shedding light on the effect of oxidized and reduced NADP/H cofactor binding on the conformational dynamics of the biocatalyst using molecular dynamics (MD) simulations. The cofactor oxidation states mainly influence the interdomain cleft region conformations of the YqhD monomers, involved in intricate cofactor binding and release. The ensemble of NADPH-bound monomers has a narrower average interdomain space resulting in more hydrogen bonds and rigid cofactor binding. NADP-bound YqhD fluctuates between open and closed conformations, while it was observed that NADPH-bound YqhD had slower opening/closing dynamics of the cofactor-binding cleft. In the light of enzyme kinetics and structural data, simulation findings have led us to postulate that the frequently sampled open conformation of the cofactor binding cleft with NADP leads to the more facile release of NADP while increased closed conformation sampling during NADPH binding enhances cofactor binding affinity and the aldehyde reductase activity of the enzyme.

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19

Verma, Rajni, Jonathan M. Ellis, and Katie R. Mitchell-Koch. "Dynamic Preference for NADP/H Cofactor Binding/Release in E. coli YqhD Oxidoreductase." Molecules 26, no. 2 (January 7, 2021): 270. http://dx.doi.org/10.3390/molecules26020270.

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YqhD, an E. coli alcohol/aldehyde oxidoreductase, is an enzyme able to produce valuable bio-renewable fuels and fine chemicals from a broad range of starting materials. Herein, we report the first computational solution-phase structure-dynamics analysis of YqhD, shedding light on the effect of oxidized and reduced NADP/H cofactor binding on the conformational dynamics of the biocatalyst using molecular dynamics (MD) simulations. The cofactor oxidation states mainly influence the interdomain cleft region conformations of the YqhD monomers, involved in intricate cofactor binding and release. The ensemble of NADPH-bound monomers has a narrower average interdomain space resulting in more hydrogen bonds and rigid cofactor binding. NADP-bound YqhD fluctuates between open and closed conformations, while it was observed that NADPH-bound YqhD had slower opening/closing dynamics of the cofactor-binding cleft. In the light of enzyme kinetics and structural data, simulation findings have led us to postulate that the frequently sampled open conformation of the cofactor binding cleft with NADP leads to the more facile release of NADP while increased closed conformation sampling during NADPH binding enhances cofactor binding affinity and the aldehyde reductase activity of the enzyme.

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20

Bray, R. C., N. A. Turner, J. Le Gall, B. A. S. Barata, and J. J. G. Moura. "Information from e.p.r. spectroscopy on the iron-sulphur centres of the iron-molybdenum protein (aldehyde oxidoreductase) of Desulfovibrio gigas." Biochemical Journal 280, no. 3 (December 15, 1991): 817–20. http://dx.doi.org/10.1042/bj2800817.

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E.p.r. spectra of reduced iron-sulphur centres of the aldehyde oxidoreductase (iron-molybdenum protein) of Desulfovibrio gigas were recorded at X-band and Q-band frequencies and simulated. Results are consistent with the view that only two types of [2Fe-2S] clusters are present, as in eukaryotic molybdenum-containing hydroxylases. The data indicate the Fe/SI centre to be very similar, and the Fe/SII centre somewhat similar, to these centres in the eukaryotic enzymes.

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21

Terao, Mineko, Enrico Garattini, Maria João Romão, and Silke Leimkühler. "Evolution, expression, and substrate specificities of aldehyde oxidase enzymes in eukaryotes." Journal of Biological Chemistry 295, no. 16 (March 6, 2020): 5377–89. http://dx.doi.org/10.1074/jbc.rev119.007741.

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Aldehyde oxidases (AOXs) are a small group of enzymes belonging to the larger family of molybdo-flavoenzymes, along with the well-characterized xanthine oxidoreductase. The two major types of reactions that are catalyzed by AOXs are the hydroxylation of heterocycles and the oxidation of aldehydes to their corresponding carboxylic acids. Different animal species have different complements of AOX genes. The two extremes are represented in humans and rodents; whereas the human genome contains a single active gene (AOX1), those of rodents, such as mice, are endowed with four genes (Aox1-4), clustering on the same chromosome, each encoding a functionally distinct AOX enzyme. It still remains enigmatic why some species have numerous AOX enzymes, whereas others harbor only one functional enzyme. At present, little is known about the physiological relevance of AOX enzymes in humans and their additional forms in other mammals. These enzymes are expressed in the liver and play an important role in the metabolisms of drugs and other xenobiotics. In this review, we discuss the expression, tissue-specific roles, and substrate specificities of the different mammalian AOX enzymes and highlight insights into their physiological roles.

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22

Thapper, Anders, Maria G. Rivas, Carlos D. Brondino, Bernard Ollivier, Guy Fauque, Isabel Moura, and José J. G. Moura. "Biochemical and spectroscopic characterization of an aldehyde oxidoreductase isolated from Desulfovibrio aminophilus." Journal of Inorganic Biochemistry 100, no. 1 (January 2006): 44–50. http://dx.doi.org/10.1016/j.jinorgbio.2005.09.013.

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23

He, Aimin, Tao Li, Lacy Daniels, Ian Fotheringham, and John P. N. Rosazza. "Nocardia sp. Carboxylic Acid Reductase: Cloning, Expression, and Characterization of a New Aldehyde Oxidoreductase Family." Applied and Environmental Microbiology 70, no. 3 (March 2004): 1874–81. http://dx.doi.org/10.1128/aem.70.3.1874-1881.2004.

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ABSTRACT We have cloned, sequenced, and expressed the gene for a unique ATP- and NADPH-dependent carboxylic acid reductase (CAR) from a Nocardia species that reduces carboxylic acids to their corresponding aldehydes. Recombinant CAR containing an N-terminal histidine affinity tag had Km values for benzoate, ATP, and NADPH that were similar to those for natural CAR, and recombinant CAR reduced benzoic, vanillic, and ferulic acids to their corresponding aldehydes. car is the first example of a new gene family encoding oxidoreductases with remote acyl adenylation and reductase sites.

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24

Lehrke, Markus, Steffen Rump, Torsten Heidenreich, Josef Wissing, Ralf R. Mendel, and Florian Bittner. "Identification of persulfide-binding and disulfide-forming cysteine residues in the NifS-like domain of the molybdenum cofactor sulfurase ABA3 by cysteine-scanning mutagenesis." Biochemical Journal 441, no. 3 (January 16, 2012): 823–39. http://dx.doi.org/10.1042/bj20111170.

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The Moco (molybdenum cofactor) sulfurase ABA3 from Arabidopsis thaliana catalyses the sulfuration of the Moco of aldehyde oxidase and xanthine oxidoreductase, which represents the final activation step of these enzymes. ABA3 consists of an N-terminal NifS-like domain that exhibits L-cysteine desulfurase activity and a C-terminal domain that binds sulfurated Moco. The strictly conserved Cys430 in the NifS-like domain binds a persulfide intermediate, which is abstracted from the substrate L-cysteine and finally needs to be transferred to the Moco of aldehyde oxidase and xanthine oxidoreductase. In addition to Cys430, another eight cysteine residues are located in the NifS-like domain, with two of them being highly conserved among Moco sulfurase proteins and, at the same time, being in close proximity to Cys430. By determination of the number of surface-exposed cysteine residues and the number of persulfide-binding cysteine residues in combination with the sequential substitution of each of the nine cysteine residues, a second persulfide-binding cysteine residue, Cys206, was identified. Furthermore, the active-site Cys430 was found to be located on top of a loop structure, formed by the two flanking residues Cys428 and Cys435, which are likely to form an intramolecular disulfide bridge. These findings are confirmed by a structural model of the NifS-like domain, which indicates that Cys428 and Cys435 are within disulfide bond distance and that a persulfide transfer from Cys430 to Cys206 is indeed possible.

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25

Wahyudi, Aris Tri, Haruko Takeyama, Yoshiko Okamura, Yorikane Fukuda, and Tadashi Matsunaga. "Characterization of aldehyde ferredoxin oxidoreductase gene defective mutant in Magnetospirillum magneticum AMB-1." Biochemical and Biophysical Research Communications 303, no. 1 (March 2003): 223–29. http://dx.doi.org/10.1016/s0006-291x(03)00303-6.

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26

Metz, Sebastian, Dongqi Wang, and Walter Thiel. "Reductive Half-Reaction of Aldehyde Oxidoreductase toward Acetaldehyde: A Combined QM/MM Study." Journal of the American Chemical Society 131, no. 13 (April 8, 2009): 4628–40. http://dx.doi.org/10.1021/ja805938w.

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27

Rebelo, J., J. Dias, R. Huber, J. Moura, and M. Romão. "Structure refinement of the aldehyde oxidoreductase from Desulfovibrio gigas (MOP) at 1.28 Å." JBIC Journal of Biological Inorganic Chemistry 6, no. 8 (October 2001): 791–800. http://dx.doi.org/10.1007/s007750100255.

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28

Zhelyaskov, Valentin, Kwok To Yue, Jean LeGall, Belarmino A. S. Barata, and JoséJ G. Moura. "Resonance Raman study on the iron-sulfur centers of Desulfovibrio gigas aldehyde oxidoreductase." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1252, no. 2 (October 1995): 300–304. http://dx.doi.org/10.1016/0167-4838(95)00116-c.

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29

Roy, Roopali, Swarnalatha Mukund, Gerrit J. Schut, Dianne M. Dunn, Robert Weiss, and Michael W. W. Adams. "Purification and Molecular Characterization of the Tungsten-Containing Formaldehyde Ferredoxin Oxidoreductase from the Hyperthermophilic Archaeon Pyrococcus furiosus: the Third of a Putative Five-Member Tungstoenzyme Family." Journal of Bacteriology 181, no. 4 (February 15, 1999): 1171–80. http://dx.doi.org/10.1128/jb.181.4.1171-1180.1999.

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ABSTRACT Pyrococcus furiosus is a hyperthermophilic archaeon which grows optimally near 100°C by fermenting peptides and sugars to produce organic acids, CO2, and H2. Its growth requires tungsten, and two different tungsten-containing enzymes, aldehyde ferredoxin oxidoreductase (AOR) and glyceraldehyde-3-phosphate ferredoxin oxidoreductase (GAPOR), have been previously purified from P. furiosus. These two enzymes are thought to function in the metabolism of peptides and carbohydrates, respectively. A third type of tungsten-containing enzyme, formaldehyde ferredoxin oxidoreductase (FOR), has now been characterized. FOR is a homotetramer with a mass of 280 kDa and contains approximately 1 W atom, 4 Fe atoms, and 1 Ca atom per subunit, together with a pterin cofactor. The low recovery of FOR activity during purification was attributed to loss of sulfide, since the purified enzyme was activated up to fivefold by treatment with sulfide (HS−) under reducing conditions. FOR usesP. furiosus ferredoxin as an electron acceptor (Km = 100 μM) and oxidizes a range of aldehydes. Formaldehyde (Km = 15 mM for the sulfide-activated enzyme) was used in routine assays, but the physiological substrate is thought to be an aliphatic C5semi- or dialdehyde, e.g., glutaric dialdehyde (Km = 1 mM). Based on its amino-terminal sequence, the gene encoding FOR (for) was identified in the genomic database, together with those encoding AOR and GAPOR. The amino acid sequence of FOR corresponded to a mass of 68.7 kDa and is highly similar to those of the subunits of AOR (61% similarity and 40% identity) and GAPOR (50% similarity and 23% identity). The three genes are not linked on the P. furiosuschromosome. Two additional (and nonlinked) genes (termedwor4 and wor5) that encode putative tungstoenzymes with 57% (WOR4) and 56% (WOR5) sequence similarity to FOR were also identified. Based on sequence motif similarities with FOR, both WOR4 and WOR5 are also proposed to contain a tungstobispterin site and one [4Fe-4S] cluster per subunit.

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30

Kletzin, A., S. Mukund, T. L. Kelley-Crouse, M. K. Chan, D. C. Rees, and M. W. Adams. "Molecular characterization of the genes encoding the tungsten-containing aldehyde ferredoxin oxidoreductase from Pyrococcus furiosus and formaldehyde ferredoxin oxidoreductase from Thermococcus litoralis." Journal of bacteriology 177, no. 16 (1995): 4817–19. http://dx.doi.org/10.1128/jb.177.16.4817-4819.1995.

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Li, Tao, and John P. N. Rosazza. "NMR Identification of an Acyl-adenylate Intermediate in the Aryl-aldehyde Oxidoreductase Catalyzed Reaction." Journal of Biological Chemistry 273, no. 51 (December 18, 1998): 34230–33. http://dx.doi.org/10.1074/jbc.273.51.34230.

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32

Hensgens, C. M., W. R. Hagen, and T. A. Hansen. "Purification and characterization of a benzylviologen-linked, tungsten-containing aldehyde oxidoreductase from Desulfovibrio gigas." Journal of bacteriology 177, no. 21 (1995): 6195–200. http://dx.doi.org/10.1128/jb.177.21.6195-6200.1995.

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33

Rebelo, Jorge, Sofia Macieira, João M. Dias, Robert Huber, Carla S. Ascenso, Frank Rusnak, José J. G. Moura, Isabel Moura, and Maria J. Romão. "Gene sequence and crystal structure of the aldehyde oxidoreductase from Desulfovibrio desulfuricans ATCC 27774." Journal of Molecular Biology 297, no. 1 (March 2000): 135–46. http://dx.doi.org/10.1006/jmbi.2000.3552.

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Romão, Maria João. "Structural insights on aldehyde oxidase and xanthine oxidoreductase and their roles in xenobiotic metabolism." Free Radical Biology and Medicine 120 (May 2018): S23. http://dx.doi.org/10.1016/j.freeradbiomed.2018.04.555.

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35

Thapper, Anders, D. R. Boer, Carlos D. Brondino, José J. G. Moura, and Maria J. Romão. "Correlating EPR and X-ray structural analysis of arsenite-inhibited forms of aldehyde oxidoreductase." JBIC Journal of Biological Inorganic Chemistry 12, no. 3 (December 1, 2006): 353–66. http://dx.doi.org/10.1007/s00775-006-0191-9.

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Songsiriritthigul, Chomphunuch, Rawint Narawongsanont, Chonticha Tantitadapitak, Hong-Hsiang Guan, and Chun-Jung Chen. "Structure–function study of AKR4C14, an aldo-keto reductase from Thai jasmine rice (Oryza sativa L. ssp. indica cv. KDML105)." Acta Crystallographica Section D Structural Biology 76, no. 5 (April 23, 2020): 472–83. http://dx.doi.org/10.1107/s2059798320004313.

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Aldo-keto reductases (AKRs) are NADPH/NADP+-dependent oxidoreductase enzymes that metabolize an aldehyde/ketone to the corresponding alcohol. AKR4C14 from rice exhibits a much higher efficiency in metabolizing malondialdehyde (MDA) than do the Arabidopsis enzymes AKR4C8 and AKR4C9, despite sharing greater than 60% amino-acid sequence identity. This study confirms the role of rice AKR4C14 in the detoxification of methylglyoxal and MDA, and demonstrates that the endogenous contents of both aldehydes in transgenic Arabidopsis ectopically expressing AKR4C14 are significantly lower than their levels in the wild type. The apo structure of indica rice AKR4C14 was also determined in the absence of the cofactor, revealing the stabilized open conformation. This is the first crystal structure in AKR subfamily 4C from rice to be observed in the apo form (without bound NADP+). The refined AKR4C14 structure reveals a stabilized open conformation of loop B, suggesting the initial phase prior to cofactor binding. Based on the X-ray crystal structure, the substrate- and cofactor-binding pockets of AKR4C14 are formed by loops A, B, C and β1α1. Moreover, the residues Ser211 and Asn220 on loop B are proposed as the hinge residues that are responsible for conformational alteration while the cofactor binds. The open conformation of loop B is proposed to involve Phe216 pointing out from the cofactor-binding site and the opening of the safety belt. Structural comparison with other AKRs in subfamily 4C emphasizes the role of the substrate-channel wall, consisting of Trp24, Trp115, Tyr206, Phe216, Leu291 and Phe295, in substrate discrimination. In particular, Leu291 could contribute greatly to substrate selectivity, explaining the preference of AKR4C14 for its straight-chain aldehyde substrate.

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Maia, Luisa B., and José J. G. Moura. "Putting xanthine oxidoreductase and aldehyde oxidase on the NO metabolism map: Nitrite reduction by molybdoenzymes." Redox Biology 19 (October 2018): 274–89. http://dx.doi.org/10.1016/j.redox.2018.08.020.

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Correia, Márcia A. S., Ana Rita Otrelo-Cardoso, Viola Schwuchow, Kajsa G. V. Sigfridsson Clauss, Michael Haumann, Maria João Romão, Silke Leimkühler, and Teresa Santos-Silva. "TheEscherichia coliPeriplasmic Aldehyde Oxidoreductase Is an Exceptional Member of the Xanthine Oxidase Family of Molybdoenzymes." ACS Chemical Biology 11, no. 10 (September 13, 2016): 2923–35. http://dx.doi.org/10.1021/acschembio.6b00572.

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Archer, M., M. J. Romco, R. Duarte, I. Moura, J. J. G. Moura, J. LeGall, P. Hof, and R. Huber. "Structure of the aldehyde oxidoreductase fromDesulfofibrio gigas: a member of the xanthine oxidase protein family." Acta Crystallographica Section A Foundations of Crystallography 52, a1 (August 8, 1996): C128. http://dx.doi.org/10.1107/s0108767396094056.

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George, Graham N., Roger C. Prince, Swarnalatha Mukund, and Michael W. W. Adams. "Aldehyde ferredoxin oxidoreductase from the hyperthermophilic archaebacterium Pyrococcus furiosus contains a tungsten oxo-thiolate center." Journal of the American Chemical Society 114, no. 9 (April 1992): 3521–23. http://dx.doi.org/10.1021/ja00035a055.

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Li, T., and J. P. Rosazza. "Purification, characterization, and properties of an aryl aldehyde oxidoreductase from Nocardia sp. strain NRRL 5646." Journal of bacteriology 179, no. 11 (1997): 3482–87. http://dx.doi.org/10.1128/jb.179.11.3482-3487.1997.

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42

Arendsen, Alexander F., Marcel de Vocht, Yvonne B. M. Bulsink, and W. R. Hagen. "Redox chemistry of biological tungsten: an EPR study of the aldehyde oxidoreductase from Pyrococcus furiosus." JBIC Journal of Biological Inorganic Chemistry 1, no. 4 (August 1996): 292–96. http://dx.doi.org/10.1007/s007750050056.

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43

Trincone, Antonio, Licia Lama, Rocco Rella, Sabato D'Auria, Carlo Antonio Raia, and Barbara Nicolaus. "Determination of hydride transfer stereospecificity of NADH-dependent alcohol-aldehyde/ketone oxidoreductase from Sulfolobus solfataricus." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1041, no. 1 (October 1990): 94–96. http://dx.doi.org/10.1016/0167-4838(90)90127-2.

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44

Scott, Israel M., Gabriel M. Rubinstein, Farris L. Poole, Gina L. Lipscomb, Gerrit J. Schut, Amanda M. Williams-Rhaesa, David M. Stevenson, Daniel Amador-Noguez, Robert M. Kelly, and Michael W. W. Adams. "The thermophilic biomass-degrading bacterium Caldicellulosiruptor bescii utilizes two enzymes to oxidize glyceraldehyde 3-phosphate during glycolysis." Journal of Biological Chemistry 294, no. 25 (May 16, 2019): 9995–10005. http://dx.doi.org/10.1074/jbc.ra118.007120.

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Caldicellulosiruptor bescii is an extremely thermophilic, cellulolytic bacterium with a growth optimum at 78 °C and is the most thermophilic cellulose degrader known. It is an attractive target for biotechnological applications, but metabolic engineering will require an in-depth understanding of its primary pathways. A previous analysis of its genome uncovered evidence that C. bescii may have a completely uncharacterized aspect to its redox metabolism, involving a tungsten-containing oxidoreductase of unknown function. Herein, we purified and characterized this new member of the aldehyde ferredoxin oxidoreductase family of tungstoenzymes. We show that it is a heterodimeric glyceraldehyde-3-phosphate (GAP) ferredoxin oxidoreductase (GOR) present not only in all known Caldicellulosiruptor species, but also in 44 mostly anaerobic bacterial genera. GOR is phylogenetically distinct from the monomeric GAP-oxidizing enzyme found previously in several Archaea. We found that its large subunit (GOR-L) contains a single tungstopterin site and one iron-sulfur [4Fe-4S] cluster, that the small subunit (GOR-S) contains four [4Fe-4S] clusters, and that GOR uses ferredoxin as an electron acceptor. Deletion of either subunit resulted in a distinct growth phenotype on both C5 and C6 sugars, with an increased lag phase, but higher cell densities. Using metabolomics and kinetic analyses, we show that GOR functions in parallel with the conventional GAP dehydrogenase, providing an alternative ferredoxin-dependent glycolytic pathway. These two pathways likely facilitate the recycling of reduced redox carriers (NADH and ferredoxin) in response to environmental H2 concentrations. This metabolic flexibility has important implications for the future engineering of this and related species.

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Buthet, Lara R., Florencia M. Bietto, José A. Castro, and Gerardo D. Castro. "Metabolism of ethanol to acetaldehyde by rat uterine horn subcellular fractions." Human & Experimental Toxicology 30, no. 11 (January 21, 2011): 1785–94. http://dx.doi.org/10.1177/0960327110396537.

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Controversial studies from others suggested that alcohol intake could be associated with some deleterious effects in the uterus. Not all the effects of alcohol drinking on female reproductive organs can be explained in terms of endocrine disturbances. Deleterious effect of alcohol or its metabolites in situ could also play a role. Accordingly, we found a metabolism of alcohol to acetaldehyde in the rat uterine horn tissue cytosolic fraction mediated by xanthine oxidoreductase, requiring a purine cosubstrate and inhibited by allopurinol. This activity was detected by histochemistry in the epithelium and aldehyde dehydrogenase activity was detected in the muscular layer and in the serosa. There was a microsomal process, not requiring NADPH and of enzymatic nature, oxygen-dependent and inhibited by diethyldithiocarbamate, diphenyleneiodonium and partially sensitive to esculetin and nordihydroguaiaretic acid. The presence of metabolic pathways in the uterine horn able to generate acetaldehyde, accompanied by a low capacity to destroy it through aldehyde dehydrogenase, led to acetaldehyde accumulation in the uterus during ethanol exposure. Results suggest that any acetaldehyde produced in situ or arriving to the uterine horn via blood would remain in this organ sufficiently to have the opportunity to react with critical molecules to cause deleterious effects.

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Barata, Belarmino A. S., Jean LeGall, and Jose J. G. Moura. "Aldehyde oxidoreductase activity in Desulfovibrio gigas: In vitro reconstitution of an electron-transfer chain from aldehydes to the production of molecular hydrogen." Biochemistry 32, no. 43 (January 26, 1993): 11559–68. http://dx.doi.org/10.1021/bi00094a012.

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Neumann, Meina, Gerd Mittelstädt, Chantal Iobbi-Nivol, Miguel Saggu, Friedhelm Lendzian, Peter Hildebrandt, and Silke Leimkühler. "A periplasmic aldehyde oxidoreductase represents the first molybdopterin cytosine dinucleotide cofactor containing molybdo-flavoenzyme fromEscherichia coli." FEBS Journal 276, no. 10 (May 2009): 2762–74. http://dx.doi.org/10.1111/j.1742-4658.2009.07000.x.

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48

Barata, Belarmino A. S., B. H. Huynh, J. LeGall, and J. J. G. Moura. "EPR and Mossbauer characterization of the aldehyde oxidoreductase from Desulfovibrio gigas: Novel strutural and physiological properties." Journal of Inorganic Biochemistry 51, no. 1-2 (July 1993): 137. http://dx.doi.org/10.1016/0162-0134(93)85173-6.

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Romão, M. J., and R. Huber. "Crystal structure and mechanism of action of the xanthine oxidase-related aldehyde oxidoreductase from Desulfovibrio gigas." Biochemical Society Transactions 25, no. 3 (August 1, 1997): 755–57. http://dx.doi.org/10.1042/bst0250755.

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50

Coyle, Christine M., Johnathan Z. Cheng, Sarah E. O'Connor, and Daniel G. Panaccione. "An Old Yellow Enzyme Gene Controls the Branch Point between Aspergillus fumigatus and Claviceps purpurea Ergot Alkaloid Pathways." Applied and Environmental Microbiology 76, no. 12 (April 30, 2010): 3898–903. http://dx.doi.org/10.1128/aem.02914-09.

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ABSTRACT Ergot fungi in the genus Claviceps and several related fungal groups in the family Clavicipitaceae produce toxic ergot alkaloids. These fungi produce a variety of ergot alkaloids, including clavines as well as lysergic acid derivatives. Ergot alkaloids are also produced by the distantly related, opportunistic human pathogen Aspergillus fumigatus. However, this fungus produces festuclavine and fumigaclavines A, B, and C, which collectively differ from clavines of clavicipitaceous fungi in saturation of the last assembled of four rings in the ergoline ring structure. The two lineages are hypothesized to share early steps of the ergot alkaloid pathway before diverging at some point after the synthesis of the tricyclic intermediate chanoclavine-I. Disruption of easA, a gene predicted to encode a flavin-dependent oxidoreductase of the old yellow enzyme class, in A. fumigatus led to accumulation of chanoclavine-I and chanoclavine-I-aldehyde. Complementation of the A. fumigatus easA mutant with a wild-type allele from the same fungus restored the wild-type profile of ergot alkaloids. These data demonstrate that the product of A. fumigatus easA is required for incorporation of chanoclavine-I-aldehyde into more-complex ergot alkaloids, presumably by reducing the double bond conjugated to the aldehyde group, thus facilitating ring closure. Augmentation of the A. fumigatus easA mutant with a homologue of easA from Claviceps purpurea resulted in accumulation of ergot alkaloids typical of clavicipitaceous fungi (agroclavine, setoclavine, and its diastereoisomer isosetoclavine). These data indicate that functional differences in the easA-encoded old yellow enzymes of A. fumigatus and C. purpurea result in divergence of their respective ergot alkaloid pathways.

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