Structure/function relationships of [NiFe]-and [FeFe]-hydrogenases

JC Fontecilla-Camps, A Volbeda, C Cavazza… - Chemical …, 2007 - ACS Publications
The utilization of hydrogen by micro-organisms as a source of reducing power or of protons
as final electron acceptors is mediated by metalloenzymes called hydrogenases. The need …

Bacterial respiration: a flexible process for a changing environment

DJ Richardson - Microbiology, 2000 - microbiologyresearch.org
The respiration of oxygen is fundamental to the life of higher animals and plants. The basic
respiratory process in the mitochondria of these organisms involves the donation of …

[图书][B] Handbook on metalloproteins

I Bertini, A Sigel - 2001 - taylorfrancis.com
This Handbook on Metalloproteins focuses on the available structural information of proteins
and their metal ion coordination spheres. It centers on the metal ions indispensable for life …

Models of the bis-histidine-ligated electron-transferring cytochromes. Comparative geometric and electronic structure of low-spin ferro-and ferrihemes

FA Walker - Chemical reviews, 2004 - ACS Publications
Models of the Bis-Histidine-Ligated Electron-Transferring Cytochromes. Comparative Geometric
and Electronic Structure of Low-Spin Ferro- and Ferrihemes | Chemical Reviews ACS ACS …

[HTML][HTML] Sulphate respiration from hydrogen in Desulfovibrio bacteria: a structural biology overview

PM Matias, IAC Pereira, CM Soares… - Progress in biophysics …, 2005 - Elsevier
Sulphate-reducing organisms are widespread in anaerobic enviroments, including the
gastrointestinal tract of man and other animals. The study of these bacteria has attracted …

Molecular Dynamics at Constant pH and Reduction Potential: Application to Cytochrome c3

M Machuqueiro, AM Baptista - Journal of the American Chemical …, 2009 - ACS Publications
Here we present a new implementation and extension of the stochastic titration method
which makes it possible to perform MD simulations at constant pH and reduction potential …

The primary and three-dimensional structures of a nine-haem cytochrome c from Desulfovibrio desulfuricans ATCC 27774 reveal a new member of the Hmc family

PM Matias, R Coelho, IAC Pereira, AV Coelho… - Structure, 1999 - cell.com
Background: Haem-containing proteins are directly involved in electron transfer as well as in
enzymatic functions. The nine-haem cytochrome c (9Hcc), previously described as having …

A Membrane‐Bound Cytochrome c3: A Type II Cytochrome c3 from Desulfovibrio vulgaris Hildenborough

FMA Valente, LM Saraiva, J LeGall, AV Xavier… - …, 2001 - Wiley Online Library
A new tetraheme cytochrome c3 was isolated from the membranes of Desulfovibrio vulgaris
Hildenborough (DvH). This cytochrome has a molecular mass of 13.4 kDa and a pI of 5.5 …

Exploring coupled redox and pH processes with a force-field-based approach: applications to five different systems

VWD Cruzeiro, GT Feliciano… - Journal of the American …, 2020 - ACS Publications
Coupled redox and pH-driven processes are at the core of many important biological
mechanisms. As the distribution of protonation and redox states in a system is associated …

Structural basis for the network of functional cooperativities in cytochrome c3 from Desulfovibrio gigas: solution structures of the oxidised and reduced states

L Brennan, DL Turner, AC Messias, ML Teodoro… - Journal of Molecular …, 2000 - Elsevier
Cytochrome c3 is a 14 kDa tetrahaem protein that plays a central role in the bioenergetic
metabolism of Desulfovibrio spp. This involves an energy transduction mechanism made …