(Q50731388)

18 March 2018

title

Redox infrared markers of the heme and axial ligands in microperoxidase: Bases for the analysis of c-type cytochromes. (English)

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18 March 2018

author

Catherine Berthomieu

series ordinal

3

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18 March 2018

Alain Boussac

series ordinal

2

object named as

Alain Boussac

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18 March 2018

author name string

Laure Marboutin

series ordinal

1

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18 March 2018

publication date

17 June 2006

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18 March 2018

Journal of Biological Inorganic Chemistry

published in

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18 March 2018

volume

11

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18 March 2018

issue

7

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18 March 2018

page(s)

811-823

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18 March 2018

https://scigraph.springernature.com/pub.10.1007/s00775-006-0119-4

exact match

0 references

cites work

N.m.r., e.p.r. and magnetic-c.d. studies of cytochrome f. Identity of the haem axial ligands

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Redox Dependent Changes at the Heme Propionates in CytochromecOxidase fromParacoccusdenitrificans: Direct Evidence from FTIR Difference Spectroscopy in Combination with Heme Propionate13C Labeling†

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Probing heme propionate involvement in transmembrane proton transfer coupled to electron transfer in dihemic quinol:fumarate reductase by 13C-labeling and FTIR difference spectroscopy

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Resonance Raman investigation of imidazole and imidazolate complexes of microperoxidase: characterization of the bis(histidine) axial ligation in c-type cytochromes

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Redox-dependent changes in .beta.-extended chain and turn structures of cytochrome c in water solution determined by second derivative amide I infrared spectra

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Structure of the Cytochrome b 6 f Complex of Oxygenic Photosynthesis: Tuning the Cavity

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N-hydroxyguanidines as new heme ligands: UV-visible, EPR, and resonance Raman studies of the interaction of various compounds bearing a C=NOH function with microperoxidase-8.

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A Fourier‐Transform Infrared Spectroscopic Investigation of the Hydrogen‐Deuterium Exchange and Secondary Structure of the 28‐kDa Channel‐Forming Integral Membrane Protein (CHIP28)

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Microperoxidase 8 adsorbed on a roughened silver electrode as a monomeric high-spin penta-coordinated species: characterization by SERR spectroscopy and electrochemistry.

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Model Systems for Interacting Heme Moieties. I. The Heme Undecapeptide of Cytochrome c

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Control of cytochrome C redox potential: axial ligation and protein environment effects

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Hemes and hemeproteins, 2: The pH-dependent equilibria of microperoxidase-8 and characterization of the coordination sphere of Fe(III)

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Spectral and redox characterization of the heme ci of the cytochrome b6f complex

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Structure of cytochrome c nitrite reductase

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Resonance Raman spectra of heme proteins. Effects of oxidation and spin state

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Bis-methionine ligation to heme iron in mutants of cytochrome b562. 1. Spectroscopic and electrochemical characterization of the electronic properties.

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Hemes and hemoproteins. 1: Preparation and analysis of the heme-containing octapeptide (microperoxidase-8) and identification of the monomeric form in aqueous solution

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12 December 2020

10.1007/S00775-006-0119-4

Identifiers

DOI

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18 March 2018

1 reference

18 March 2018