2001
DOI: 10.1074/jbc.m107136200
|View full text |Cite
|
Sign up to set email alerts
|

Abstract: Cell metabolism relies on energy transduction usually performed by complex membrane-spanning proteins that couple different chemical processes, e.g. electron and proton transfer in proton-pumps. There is great interest in determining at the molecular level the structural details that control these energy transduction events, particularly those involving multiple electrons and protons, because tight control is required to avoid the production of dangerous reactive intermediates. Tetraheme cytochrome c 3 is a sm… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1
1

Citation Types

6
68
0

Year Published

2002
2002
2023
2023

Publication Types

Select...
4
3
1

Relationship

4
4

Authors

Journals

citations
Cited by 39 publications
(74 citation statements)
references
References 43 publications
6
68
0
Order By: Relevance
“…2 as a function of the solution potential for the experiments performed at pH 6.3, 7.4 and 8. 4. This shows that the reduction potentials are pH dependent and cover a wide range of values, as expected for a multiredox centre protein.…”
Section: Visible Redox Titrationsmentioning
confidence: 76%
See 1 more Smart Citation
“…2 as a function of the solution potential for the experiments performed at pH 6.3, 7.4 and 8. 4. This shows that the reduction potentials are pH dependent and cover a wide range of values, as expected for a multiredox centre protein.…”
Section: Visible Redox Titrationsmentioning
confidence: 76%
“…A large variety of multi-haem c -type cytochromes is found in the periplasmic space of sulfate reducing bacteria (SRB) and a soluble monomeric tetrahaem cytochrome (cyt c 3 ) has been the focus of the most detailed studies [3,4]. A nine-haem cytochrome c (9Hcc), isolated from the SRB Desulfovibrio desulfuricans ATCC 27774 (Dd 27774) [5] is a 37.8 kDa monomeric protein [6] containing 292 aminoacid residues.…”
Section: Introductionmentioning
confidence: 99%
“…It is reasonable to assume that this small but complex molecule has evolved to a high degree of efficiency to carry both the protons and the electrons generated from the oxidation of hydrogen. Although at present there is no experimental evidence for a second proton-binding site, an extra proton could be accommodated through small changes in the populations at a number of other sites and assist the two-electron transfer as seen in cytochrome c 3 from D. desulfuricans 27774 (15,16). It is likely that the changes in thermodynamic parameters that occur when the transducer donor-acceptor complex is formed will improve the functional properties.…”
Section: Structural Interpretation Of the Thermodynamic Properties-mentioning
confidence: 99%
“…In these cytochromes an antielectrostatic (conformationally mediated)-positive homotropic cooperativity between two hemes governs a coordinated twoelectron transfer, whereas a positive redox-Bohr effect controls their proton thrusting activity. Subsequent characterization of the cytochrome c 3 from Desulfovibrio desulfuricans ATCC 27774 (15,16) illustrated yet another mechanism to facilitate a coordinated two-electron transfer even when there are no positive homotropic redox cooperativities. This alternative mech-anism is achieved by the concerted effect of two positive redoxBohr effects governing a proton-assisted coordinated twoelectron transfer.…”
mentioning
confidence: 99%
“…The bacteria of this genus are characterized by having an unusual number of periplasmic multiheme cytochromes, of which the most abundant and widespread is the well characterized tetraheme Type I cytochrome c 3 (TpI-c 3 ) (9), which is thought to play a central role in the respiratory chain and act as a physiological partner for hydrogenases. Other examples include the sixteen-heme high molecular mass cytochrome c (HmcA) (10 -14), the nineheme cytochrome c (9HcA) (15)(16)(17), the tetraheme type II cytochrome c 3 (TpII-c 3 ), which differs from the TpI-c 3 in structural, functional, and genetic terms (18), the octaheme cytochrome c 3 (M r 26,000), a dimer of a tetraheme subunit (19), and the dimeric split-Soret cytochrome c, which is a dimer of a diheme subunit (20).…”
mentioning
confidence: 99%