Characterization of a synthetic peroxodiiron(III) protein model complex by nuclear resonance vibrational spectroscopy. - Wikidata - awgldk - TriplyDB

Characterization of a synthetic peroxodiiron(III) protein model complex by nuclear resonance vibrational spectroscopy.

Characterization of a synthetic peroxodiiron(III) protein model complex by nuclear resonance vibrational spectroscopy.

http://www.wikidata.org/entity/Q35243682

about

Nitrosylation of Nitric-Oxide-Sensing Regulatory Proteins Containing [4Fe-4S] Clusters Gives Rise to Multiple Iron-Nitrosyl Complexes.A strenuous experimental journey searching for spectroscopic evidence of a bridging nickel-iron-hydride in [NiFe] hydrogenase.Energy calibration issues in nuclear resonant vibrational spectroscopy: observing small spectral shifts and making fast calibrations.

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P2860

Characterization of a synthetic peroxodiiron(III) protein model complex by nuclear resonance vibrational spectroscopy.

http://www.wikidata.org/entity/Q35243682

description

2011 nî lūn-bûn

@nan

2011 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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name

Characterization of a syntheti ...... ance vibrational spectroscopy.

@ast

Characterization of a syntheti ...... ance vibrational spectroscopy.

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type

label

Characterization of a syntheti ...... ance vibrational spectroscopy.

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Characterization of a syntheti ...... ance vibrational spectroscopy.

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prefLabel

Characterization of a syntheti ...... ance vibrational spectroscopy.

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Characterization of a syntheti ...... ance vibrational spectroscopy.

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Chemical Communications

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Characterization of a syntheti ...... ance vibrational spectroscopy.

@en

P2093

Christine E Tinberg

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Eric Dowty

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Hongxin Wang

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Loi H Do

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Stephen P Cramer

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Yoshitaka Yoda

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P2860

Crystallographic and catalytic studies of the peroxide-shunt reaction in a diiron hydroxylase

Expression and purification of the recombinant subunits of toluene/o-xylene monooxygenase and reconstitution of the active complex.

Carboxylate as the protonation site in (Peroxo)diiron(III) model complexes of soluble methane monooxygenase and related diiron proteins.

Characterization of two distinct adducts in the reaction of a nonheme diiron(II) complex with O2.

Nuclear resonance vibrational spectroscopy applied to [Fe(OEP)(NO)]: the vibrational assignments of five-coordinate ferrous heme-nitrosyls and implications for electronic structure.

Identification of protein-bound dinitrosyl iron complexes by nuclear resonance vibrational spectroscopy

Dioxygen Activation and Methane Hydroxylation by Soluble Methane Monooxygenase: A Tale of Two Irons and Three Proteins A list of abbreviations can be found in Section 7.

Characterization of iron dinitrosyl species formed in the reaction of nitric oxide with a biological Rieske center

Definition of the intermediates and mechanism of the anticancer drug bleomycin using nuclear resonance vibrational spectroscopy and related methods.

Dioxygen activation in soluble methane monooxygenase

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10945-10947

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scholarly article

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10.1039/C1CC13836G

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39

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Stephen J. Lippard

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2011-09-06T00:00:00Z

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51625173

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21897991

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3183359

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