Intramolecular electron transfer in ferredoxin II from Desulfovibrio desulfuricans Norway

Blanchard, Laurence; Payan, F.; Mei, Qian; Haser, R.; Noailly, Michèle; Bruschi, Mireille; Guerlesquin, Françoise

doi:10.1016/0005-2728(93)90165-c

Cited by 10 publications

(5 citation statements)

References 28 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Intramolecular electron transfer between the two clusters has been characterized and can be very different from one ferredoxin to another ( − ). Moreover, it is not clearly known whether the two clusters are equivalent in their interactions with redox partners ( , ), although they exhibit differential reactivities toward small electron donors or oxidants ( , ). Thus PSI constitutes the only case in which both clusters are shown to be essential for the functionality of the protein.…”

Section: Discussionmentioning

confidence: 99%

Electron Transfer in Photosystem I Reaction Centers Follows a Linear Pathway in Which Iron−Sulfur Cluster F_B Is the Immediate Electron Donor to Soluble Ferredoxin

et al. 1998

View full text Add to dashboard Cite

Reaction centers of photosystem I contain three different [4Fe-4S] clusters named FX, FA, and FB. The terminal photosystem I acceptors (FA, FB) are distributed asymmetrically along the membrane normal, with one of them (FA or FB) being reduced from FX and the other one (FB or FA) reducing soluble ferredoxin. In the present work, kinetics of electron transfer has been measured in PSI from the cyanobacterium Synechocystis sp. PCC 6803 after inactivation of FB by treatment with HgCl2. Photovoltage measurements indicate that, in the absence of FB, reduction of FA by FX is still faster than the rate of FX reduction [(210 ns)-1]. Flash-absorption measurements show that the affinity of ferredoxin for HgCl2-treated PSI is only decreased by a factor of 3-4 compared to untreated photosystem I. The first-order rate of ferredoxin reduction by FA-, within the photosystem I/ferredoxin complex, has been calculated from measurements of P700+ decay. Compared to control PSI, this rate is several orders of magnitude smaller (6 s-1 versus 10(4)-10(6) s-1). Moreover, it is smaller than the rate of recombination from FA-, resulting in inefficient ferredoxin reduction (yield of 25%). After reconstitution of FB, about half of the reconstituted photosystem I reaction centers recover fast reduction of ferredoxin with kinetics similar to that of untreated photosystem I. These results support FB as the direct partner of ferredoxin and as the more distal cluster of photosystem I with respect to the thylakoid membrane, in accordance with a linear electron-transfer pathway FX-->FA-->FB-->ferredoxin.

show abstract

Section: Discussionmentioning

confidence: 99%

Electron Transfer in Photosystem I Reaction Centers Follows a Linear Pathway in Which Iron−Sulfur Cluster F_B Is the Immediate Electron Donor to Soluble Ferredoxin

et al. 1998

View full text Add to dashboard Cite

show abstract

“…Dn FdxI, a 6.2 kDa protein containing a [4Fe-4S] cluster, is an obligate intermediate in DvH Cc 553 reduction by pyruvate dehydrogenase (Blanchard et al, 1993). For this reason, Dn FdxI has been chosen as a model for the 'ferredoxin-like' domain of FDH and Fe-Hase, to study the general features of the recognition between Cc 553 and its redox partners.…”

Section: Cytochrome C 553 Complexes With Ferredoxin I and [Fe]-hydrogmentioning

confidence: 99%

Transient complexes of redox proteins: structural and dynamic details from NMR studies

Prudêncio

Ubbink

2004

J of Molecular Recognition

View full text Add to dashboard Cite

Redox proteins participate in many metabolic routes, in particular those related to energy conversion. Protein-protein complexes of redox proteins are characterized by a weak affinity and a short lifetime. Two-dimensional NMR spectroscopy has been applied to many redox protein complexes, providing a wealth of information about the process of complex formation, the nature of the interface and the dynamic properties of the complex. These studies have shown that some complexes are non-specific and exist as a dynamic ensemble of orientations while in other complexes the proteins assume a single orientation. The binding interface in these complexes consists of a small hydrophobic patch for specificity, surrounded by polar, uncharged residues that may enhance dissociation, and, in most complexes, a ring or patch of charged residues that enhances the association by electrostatic interactions. The entry and exit port of the electrons is located within the hydrophobic interaction site, ensuring rapid electron transfer from one redox centre to the next.

show abstract

“…The cytochrome c 3 interactions with various electron carriers, mainly ferredoxin, − flavodoxin, , and rubredoxin have been studied by NMR due to their possible physiological roles. A recently reported method, using heteronuclear NMR and docking calculations, was used for building structural models of the cytochrome c 3 /hydrogenase electron-transfer complex (Figure ) .…”

Section: 6 Cytochrome C 3−protein Interactionsmentioning

confidence: 99%

Mechanism of Electron Transfer in Heme Proteins and Models: The NMR Approach

Simonneaux

Bondon

2005

Chem. Rev.

View full text Add to dashboard Cite

Intramolecular electron transfer in ferredoxin II from Desulfovibrio desulfuricans Norway

Cited by 10 publications

References 28 publications

Electron Transfer in Photosystem I Reaction Centers Follows a Linear Pathway in Which Iron−Sulfur Cluster F_B Is the Immediate Electron Donor to Soluble Ferredoxin

Electron Transfer in Photosystem I Reaction Centers Follows a Linear Pathway in Which Iron−Sulfur Cluster F_B Is the Immediate Electron Donor to Soluble Ferredoxin

Transient complexes of redox proteins: structural and dynamic details from NMR studies

Mechanism of Electron Transfer in Heme Proteins and Models: The NMR Approach

Contact Info

Product

Resources

About

Intramolecular electron transfer in ferredoxin II from Desulfovibrio desulfuricans Norway

Cited by 10 publications

References 28 publications

Electron Transfer in Photosystem I Reaction Centers Follows a Linear Pathway in Which Iron−Sulfur Cluster FB Is the Immediate Electron Donor to Soluble Ferredoxin

Electron Transfer in Photosystem I Reaction Centers Follows a Linear Pathway in Which Iron−Sulfur Cluster FB Is the Immediate Electron Donor to Soluble Ferredoxin

Transient complexes of redox proteins: structural and dynamic details from NMR studies

Mechanism of Electron Transfer in Heme Proteins and Models: The NMR Approach

Contact Info

Product

Resources

About

Electron Transfer in Photosystem I Reaction Centers Follows a Linear Pathway in Which Iron−Sulfur Cluster F_B Is the Immediate Electron Donor to Soluble Ferredoxin

Electron Transfer in Photosystem I Reaction Centers Follows a Linear Pathway in Which Iron−Sulfur Cluster F_B Is the Immediate Electron Donor to Soluble Ferredoxin