Involvement of a Glu71–Arg64 Couple in the Access Channel for NADH in Cytochrome P450nor

Su, Fei; Fushinobu, Shinya; Takaya, Naoki; Shoun, Hirofumi

doi:10.1271/bbb.68.1156

Cited by 7 publications

(4 citation statements)

References 9 publications

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“…The E71A mutation blocked the I-formation step as well as decreased the binding affinity for an NAD analogue dinucleotide. 29 These mutant analyses results are consistent with the present structural results. Glu71 seems to pull and fix Arg64 on NAAD binding (Figure 2), and thus to be important for the cofactor binding.…”

Section: Discussionsupporting

confidence: 93%

Structural Evidence for Direct Hydride Transfer from NADH to Cytochrome P450nor

Oshima

Fushinobu

et al. 2004

Journal of Molecular Biology

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Section: Discussionsupporting

confidence: 93%

Structural Evidence for Direct Hydride Transfer from NADH to Cytochrome P450nor

Oshima

Fushinobu

et al. 2004

Journal of Molecular Biology

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“…Significance of Glu71, according to our results, might be attributed to fixing the members of helix B 0 and thus hindering the exit of the cofactor-reforming of the triad would result in liberation of helix B 0 and acceleration of cofactor release. Observations such that E71A mutation impairs enzyme function by blocking NADH binding [40], or that in D88A and D88V mutants Nor activity considerably decreased through impairing NAD + release [38] further support our results.…”

Section: Discussionsupporting

confidence: 88%

Binding mode analysis of the NADH cofactor in nitric oxide reductase: A theoretical study

Menyhárd

Keserü

2006

Journal of Molecular Graphics and Modelling

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“…Two Arg residues, Arg64 and Arg174, play a key role in the binding [41] by putting the pyrophosphate moiety of NAAD between them. Glu71, Arg64 and Asp88 form a salt bridge network to stabilize the protein structure [44,47]. The interaction between Arg64 and Asp88 is broken upon binding of NAAD to destabilize the protein.…”

Section: Cytochrome P450nor (Fungal Nitric Oxide Reductase)mentioning

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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219

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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Involvement of a Glu71–Arg64 Couple in the Access Channel for NADH in Cytochrome P450nor

Cited by 7 publications

References 9 publications

Structural Evidence for Direct Hydride Transfer from NADH to Cytochrome P450nor

Structural Evidence for Direct Hydride Transfer from NADH to Cytochrome P450nor

Binding mode analysis of the NADH cofactor in nitric oxide reductase: A theoretical study

Fungal denitrification and nitric oxide reductase cytochrome P450nor

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