Structural Evidence for Direct Hydride Transfer from NADH to Cytochrome P450nor

Oshima, Rieko; Fushinobu, Shinya; Su, Fei; Zhang, Li; Takaya, Naoki; Shoun, Hirofumi

doi:10.1016/j.jmb.2004.07.009

Cited by 73 publications

(83 citation statements)

References 40 publications

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“…Reduction of NO ⅐ in mitochondria may also serve to prevent its action as a respiratory chain inhibitor. Bypassing the need for electron transfer reactions involving partner proteins helps to enable the fast reaction rates of NO ⅐ reduction (Ͼ10 3 s Ϫ1 ) observed for CYP55A1 (90).…”

Section: P450s Acting Independently Of Redox Partner Proteinsmentioning

confidence: 99%

Unusual Cytochrome P450 Enzymes and Reactions

Guengerich

Munro

2013

Journal of Biological Chemistry

291

217

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Cytochrome P450 enzymes primarily catalyze mixed-function oxidation reactions, plus some reductions and rearrangements of oxygenated species, e.g. prostaglandins. Most of these reactions can be rationalized in a paradigm involving Compound I, a high-valent iron-oxygen complex (FeO 3؉ ), to explain seemingly unusual reactions, including ring couplings, ring expansion and contraction, and fusion of substrates. Most P450s interact with flavoenzymes or iron-sulfur proteins to receive electrons from NAD(P)H. In some cases, P450s are fused to protein partners. Other P450s catalyze non-redox isomerization reactions. A number of permutations on the P450 theme reveal the diversity of cytochrome P450 form and function.

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Section: P450s Acting Independently Of Redox Partner Proteinsmentioning

confidence: 99%

Unusual Cytochrome P450 Enzymes and Reactions

Guengerich

Munro

2013

Journal of Biological Chemistry

291

217

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“…21) Xray crystallography of F. oxysporum P450nor ligated to NO has provided structural insight into the reaction cycle. 22,23) Since P450nor is unique among known hemoproteins in that NADH directly transfers electrons to heme, the mechanism of NADH recognition by the enzyme is intriguing. Hence several mutant proteins were prepared by site-directed mutagenesis and their ability to recognize NADH was analyzed.…”

Section: No Reductionmentioning

confidence: 99%

“…Structural analysis of P450nor complexed with an NADH analog later confirmed these findings. 23) P450nor uses NADH and NADPH as electron donors, the extent differing according to the P450nor species. This preference was investigated using mutant enzymes.…”

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confidence: 99%

Response to Hypoxia, Reduction of Electron Acceptors, and Subsequent Survival by Filamentous Fungi

Takaya

2009

Bioscience, Biotechnology, and Biochemistry

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“…The structure of I (444 nm species) as an Fe 3þ -hydroxylamine radical complex was proposed by Daiber et al [35]. dinucleotide; NAAD) [43]. The structure of the P450nor -NAAD complex is compared with that of the ferric -NO complex of P450nor [45] in figure 6.…”

mentioning

confidence: 93%

“…In P450nor2 of C. tonkinense, Ser75 is replaced with Gly, permitting accommodation of NADPH. Double mutation at these sites in P450nor of F. oxysporum (S73G/S75G; GG mutant) markedly improved the specificity against NADPH [43].…”

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confidence: 99%

Fungal denitrification and nitric oxide reductase cytochrome P450nor

Shoun

Fushinobu

Jiang

et al. 2012

Phil. Trans. R. Soc. B

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211

189

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We have shown that many fungi (eukaryotes) exhibit distinct denitrifying activities, although occurrence of denitrification was previously thought to be restricted to bacteria (prokaryotes), and have characterized the fungal denitrification system. It comprises NirK (copper-containing nitrite reductase) and P450nor (a cytochrome P450 nitric oxide (NO) reductase (Nor)) to reduce nitrite to nitrous oxide (N 2 O). The system is localized in mitochondria functioning during anaerobic respiration. Some fungal systems further contain and use dissimilatory and assimilatory nitrate reductases to denitrify nitrate. Phylogenetic analysis of nirK genes showed that the fungal-denitrifying system has the same ancestor as the bacterial counterpart and suggested a possibility of its proto-mitochondrial origin. By contrast, fungi that have acquired a P450 from bacteria by horizontal transfer of the gene, modulated its function to give a Nor activity replacing the original Nor with P450nor. P450nor receives electrons directly from nicotinamide adenine dinucleotide to reduce NO to N 2 O. The mechanism of this unprecedented electron transfer has been extensively studied and thoroughly elucidated. Fungal denitrification is often accompanied by a unique phenomenon, co-denitrification, in which a hybrid N 2 or N 2 O species is formed upon the combination of nitrogen atoms of nitrite with a nitrogen donor (amines and imines). Possible involvement of NirK and P450nor is suggested.

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Structural Evidence for Direct Hydride Transfer from NADH to Cytochrome P450nor

Cited by 73 publications

References 40 publications

Unusual Cytochrome P450 Enzymes and Reactions

Unusual Cytochrome P450 Enzymes and Reactions

Response to Hypoxia, Reduction of Electron Acceptors, and Subsequent Survival by Filamentous Fungi

Fungal denitrification and nitric oxide reductase cytochrome P450nor

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