(Q47798662)

5 February 2018

title

Roles of negatively charged surface residues of putidaredoxin in interactions with redox partners in p450cam monooxygenase system (English)

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5 February 2018

author

Koichiro Ishimori

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ORCID Public Data File 2021

author name string

M Aoki

series ordinal

1

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5 February 2018

K Ishimori

series ordinal

2

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5 February 2018

I Morishima

series ordinal

3

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5 February 2018

publication date

1 July 1998

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5 February 2018

Biochimica et Biophysica Acta

published in

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5 February 2018

volume

1386

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5 February 2018

issue

1

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5 February 2018

page(s)

157-167

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5 February 2018

Probing the interactions of putidaredoxin with redox partners in camphor P450 5-monooxygenase by mutagenesis of surface residues

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1H NMR identification of a beta-sheet structure and description of folding topology in putidaredoxin

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1H NMR sequential assignments and identification of secondary structural elements in oxidized putidaredoxin, an electron-transfer protein from Pseudomonas

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7 January 2021

An NMR-derived model for the solution structure of oxidized putidaredoxin, a 2-Fe, 2-S ferredoxin from Pseudomonas

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7 January 2021

Redox-dependent 1H NMR spectral features and tertiary structural constraints on the C-terminal region of putidaredoxin

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7 January 2021

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7 January 2021

A structure-based model for cytochrome P450cam-putidaredoxin interactions

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7 January 2021

A Role of the Putidaredoxin COOH-terminus in P -450 cam (Cytochrome m ) Hydroxylations

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7 January 2021

Putidaredoxin reduction of cytochrome P-450cam: dependence of electron transfer on the identity of putidaredoxin's C-terminal amino acid

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7 January 2021

Genetic variants in the putidaredoxin-cytochrome P-450cam electron-transfer complex: identification of the residue responsible for redox-state-dependent conformers

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Bacterial P-450cam methylene monooxygenase components: cytochrome m, putidaredoxin, and putidaredoxin reductase

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Structural characterization of lactoperoxidase in the heme environment by proton NMR spectroscopy

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7 January 2021

Iron-ligand structure and iron redox property of nitric oxide reductase cytochrome P450nor from Fusarium oxysporum: relevance to its NO reduction activity

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7 January 2021

A thermodynamic model of regulation: modulation of redox equilibria in camphor monoxygenase

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7 January 2021

Electron transfers in chemistry and biology

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7 January 2021

On the structure of the iron-sulfur complex in the two-iron ferredoxins

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7 January 2021

Proton NMR spectra of vertebrate iron-sulfur [2Fe-2S] ferredoxins. Hyperfine resonances suggest different electron delocalization patterns from plant ferredoxins

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7 January 2021

Nuclear magnetic resonance of paramagnetic metalloproteins

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7 January 2021

The reduction of putidaredoxin reductase by reduced pyridine nucleotides

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7 January 2021

The oxidation of reduced putidaredoxin reductase by oxidized putidaredoxin

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7 January 2021

The cytochrome P-450cam binding surface as defined by site-directed mutagenesis and electrostatic modeling

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7 January 2021

Putative functions of phenylalanine-350 of Pseudomonas putida cytochrome P-450cam.

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7 January 2021

Mutated forms of the [2Fe-2S] ferredoxin from Clostridium pasteurianum with noncysteinyl ligands to the iron-sulfur cluster.

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7 January 2021

Isothermal titration calorimetric studies on the associations of putidaredoxin to NADH-putidaredoxin reductase and P450cam

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7 January 2021

Thermodynamics of protein association reactions: forces contributing to stability

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7 January 2021

Thermodynamics of ferredoxin binding to ferredoxin:NADP+ reductase and the role of water at the complex interface

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7 January 2021

Binding of ferredoxin to ferredoxin:NADP+ oxidoreductase: the role of carboxyl groups, electrostatic surface potential, and molecular dipole moment

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7 January 2021

Isothermal titration calorimetric study of the association of hen egg lysozyme and the anti-lysozyme antibody HyHEL-5.

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7 January 2021

Site-specific mutagenesis demonstrates that the structural requirements for efficient electron transfer in Anabaena ferredoxin and flavodoxin are highly dependent on the reaction partner: kinetic studies with photosystem I, ferredoxin:NADP+ reductas

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7 January 2021

10.1016/S0167-4838(98)00094-6

Identifiers

DOI

1 reference

5 February 2018

1 reference

5 February 2018