Electron Transfer from HiPIP to the Photooxidized Tetraheme Cytochrome Subunit of Allochromatium vinosum Reaction Center: New Insights from Site-Directed Mutagenesis and Computational Studies-Reference-Cited by-同舟云学术

Electron Transfer from HiPIP to the Photooxidized Tetraheme Cytochrome Subunit of Allochromatium vinosum Reaction Center: New Insights from Site-Directed Mutagenesis and Computational Studies

Published:2003-12-20 Issue:2 Volume:43 Page:437-445
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Venturoli Giovanni¹,Mamedov Mahir D.¹,Mansy Sheref S.¹,Musiani Francesco¹,Strocchi Massimo¹,Francia Francesco¹,Semenov Alexey Yu.¹,Cowan James A.¹,Ciurli Stefano¹

Affiliation:

1. Laboratorio di Biochimica e Biofisica, Dipartimento di Biologia, Università di Bologna, Bologna, Italy, Istituto Nazionale per la Fisica della Materia (INFM), UdR di Bologna, Bologna, Italy, A. N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow, Russia, Department of Chemistry, Ohio State University, Columbus, Ohio, USA, and Department of Agro-Environmental Science and Technology, University of Bologna, Bologna, Italy

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi035384v

Reference76 articles.

1. X-ray Structure Determination of the Cytochrome c2: Reaction Center Electron Transfer Complex from Rhodobacter sphaeroides

2. X-ray structure analysis of a membrane protein complex

3. Electrogenic steps in the redox reactions catalyzed by photosynthetic reaction-centre complex from Rhodopseudomonas viridis

Cited by 9 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Genomic Comparison, Phylogeny and Taxonomic Reevaluation of the Ectothiorhodospiraceae and Description of Halorhodospiraceae fam. nov. and Halochlorospira gen. nov.;Microorganisms;2022-01-26

2. Crystal structure of a photosynthetic LH1-RC in complex with its electron donor HiPIP;Nature Communications;2021-02-17

3. Crystallographic characterization of the high-potential iron-sulfur protein in the oxidized state at 0.8 Å resolution;PLOS ONE;2017-05-22

4. Analysis of the complex formation, interaction and electron transfer pathway between the “open” conformation of NADPH-cytochrome P450 reductase and aromatase;Steroids;2015-09

5. High potential iron–sulfur proteins and their role as soluble electron carriers in bacterial photosynthesis: tale of a discovery;Photosynthesis Research;2005-07