NDLI: Monooxygenation by a thermophilic cytochrome P450 via direct electron donation from NADH

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Reorientation of cytochrome c₂ upon interaction with oppositely charged macromolecules probed by SR EPR: implications for the role of dipole moment to facilitate collisions in proper configuration for electron transfer

Control of the stereo-selectivity of styrene epoxidation by cytochrome P450 BM3 using structure-based mutagenesis

Circular dichroism spectra of cytochrome c oxidase

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Metallomics Vol - 3 Issue - 3

Metallomics Vol - 3 Issue - 2

Metallomics Vol -2

Metallomics Vol -1

Monooxygenation by a thermophilic cytochrome P450 via direct electron donation from NADH

Content Provider	Royal Society of Chemistry (RSC)
Author	Yohda, Masafumi Matsuda, Keisuke Yoshida, Hiromi Kamitori, Shigehiro Nakamura, Nobuhumi Ohtaki, Akashi Matsumura, Hirotoshi Ohno, Hiroyuki
Copyright Year	2011
Abstract	The catalysis of cytochrome P450s requires two-electron donation for the activation of an oxygen molecule. Here, we report the enzymatic catalysis of cytochrome P450, CYP119A2 (P450st), from a thermoacidophilic crenarchaeon, Sulfolobus tokodaii strain 7, with NAD(P)H as an electron donor and no redox partners and the crystallographic analysis of P450st at high resolution. P450st can catalyse styrene epoxidation with either NADH or NADPH as an electron donor. The P450st reaction with NADH exhibited a sequential mechanism. X-ray crystallography at a resolution of 1.94 Å revealed a sufficiently large heme pocket for NAD(P)H binding and a novel contiguous channel from the active site to bulk solvent in the distal heme pocket. The narrow channel may transfer protons or water to the heme pocket even when a bulky compound, such as NAD(P)H, binds in the pocket. In addition, the F/G loop region (Leu151-Glu156), located around the substrate channel, was deleted in the mutant and constructed to improve the accessibility of NAD(P)H to the heme pocket. Kinetic properties of the Δ151-156 mutant were compared with those of the wild-type P450st. The Km value of the mutant was about 2 times lower than that of the wild-type. The results indicated that NAD(P)H could provide the electrons for P450st within the heme pocket.
Starting Page	389
Ending Page	395
Page Count	7
File Format	HTM / HTML PDF
ISSN	17565901
Volume Number	3
Issue Number	4
Journal	Metallomics
DOI	10.1039/c0mt00079e
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Allotropes of oxygen Cytochrome P450 Active site Redox Sulfolobus X-ray crystallography NADH Nicotinamide adenine dinucleotide phosphate Styrene Epoxide Nicotinamide adenine dinucleotide Thermoacidophile Mutation Solvent
Content Type	Text
Resource Type	Article
Subject	Chemistry Medicine Metals and Alloys Biochemistry Biomaterials Biophysics

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Control of the stereo-selectivity of styrene epoxidation by cytochrome P450 BM3 using structure-based mutagenesis

Extraction and Quantitation of Nicotinamide Adenine Dinucleotide Redox Cofactors.

Characterization of a novel nicotinamide adenine dinucleotide-cytochrome b5 reductase mutation associated with canine hereditary methemoglobinemia.

Cytochrome P450 CYP2E1, But Not Nicotinamide Adenine Dinucleotide Phosphate Oxidase, Is Required for Ethanol-Induced Oxidative DNA Damage in Rodent Liver

Inhibition of respiratory Complex I by copper(ii)-bis(thiosemicarbazonato) complexes

Activity coupling and complex formation between bacterial luciferase and flavin reductases

Bax inhibitor 1 regulates ER-stress-induced ROS accumulation through the regulation of cytochrome P450 2E1

Pathways Linking Nicotinamide Adenine Dinucleotide Phosphate Production to Endoplasmic Reticulum Protein Oxidation and Stress

Cytochrome P450 CYP2E1, but not nicotinamide adenine dinucleotide phosphate oxidase, is required for ethanol-induced oxidative DNA damage in rodent liver.

Monooxygenation by a thermophilic cytochrome P450 via direct electron donation from NADH

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Control of the stereo-selectivity of styrene epoxidation by cytochrome P450 BM3 using structure-based mutagenesis

Extraction and Quantitation of Nicotinamide Adenine Dinucleotide Redox Cofactors.

Characterization of a novel nicotinamide adenine dinucleotide-cytochrome b5 reductase mutation associated with canine hereditary methemoglobinemia.

Cytochrome P450 CYP2E1, But Not Nicotinamide Adenine Dinucleotide Phosphate Oxidase, Is Required for Ethanol-Induced Oxidative DNA Damage in Rodent Liver

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Monooxygenation by a thermophilic cytochrome P450 via direct electron donation from NADH