A complex formation of the adrenal iron-sulfur protein (adrenodoxin) with cytochrome C and the decomposition of the iron-sulfur center

FEBS Letters ◽

10.1016/0014-5793(74)80437-0 ◽

1974 ◽

Vol 47 (1) ◽

pp. 113-116 ◽

Author(s):

Takashi Manabe ◽

Tokuji Kimura

Keyword(s):

Cytochrome C ◽

Complex Formation ◽

Iron Sulfur ◽

Iron Sulfur Center ◽

Sulfur Protein ◽

Iron Sulfur Protein

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Faculty Opinions recommendation of Redox-dependent complex formation by an ATP-dependent activator of the corrinoid/iron-sulfur protein.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.14264957.15779244 ◽

2012 ◽

Author(s):

Rowena Matthews

Keyword(s):

Complex Formation ◽

Iron Sulfur ◽

Sulfur Protein ◽

Iron Sulfur Protein

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Faculty Opinions recommendation of Redox-dependent complex formation by an ATP-dependent activator of the corrinoid/iron-sulfur protein.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.14264957.15777402 ◽

2012 ◽

Author(s):

Russ Hille

Keyword(s):

Complex Formation ◽

Iron Sulfur ◽

Sulfur Protein ◽

Iron Sulfur Protein

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Significance of the “Rieske” iron-sulfur protein for formation and function of the ubiquinol-oxidation pocket of mitochondrial cytochrome c reductase (bc1 complex).

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)54876-6 ◽

1991 ◽

Vol 266 (30) ◽

pp. 19958-19964

Author(s):

U. Brandt ◽

U. Haase ◽

H. Schägger ◽

G. von Jagow

Keyword(s):

Cytochrome C ◽

Mitochondrial Cytochrome ◽

Bc1 Complex ◽

Cytochrome C Reductase ◽

Iron Sulfur ◽

Sulfur Protein ◽

Iron Sulfur Protein ◽

Rieske Iron Sulfur Protein ◽

And Function ◽

Mitochondrial Cytochrome C

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Identification of a stable ubisemiquinone and characterization of the effects of ubiquinone oxidation-reduction status on the Rieske iron-sulfur protein in the three-subunit ubiquinol-cytochrome c oxidoreductase complex of Paracoccus denitrificans.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)47471-6 ◽

1987 ◽

Vol 262 (18) ◽

pp. 8702-8706 ◽

Author(s):

S W Meinhardt ◽

X H Yang ◽

B L Trumpower ◽

T Ohnishi

Keyword(s):

Cytochrome C ◽

Paracoccus Denitrificans ◽

Iron Sulfur ◽

Oxidation Reduction ◽

Sulfur Protein ◽

Iron Sulfur Protein ◽

Rieske Iron Sulfur Protein

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Two distinct binding sites for high potential iron-sulfur protein and cytochrome c on the reaction center-bound cytochrome of Rubrivivax gelatinosus.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(20)72574-3 ◽

2004 ◽

Vol 279 (44) ◽

pp. 46350

Author(s):

Jean Alric ◽

Makoto Yoshida ◽

Kenji V.P. Nagashima ◽

Rainer Hienerwadel ◽

Pierre Parot ◽

...

Keyword(s):

Cytochrome C ◽

Reaction Center ◽

Binding Sites ◽

High Potential ◽

Iron Sulfur ◽

Sulfur Protein ◽

Iron Sulfur Protein ◽

Rubrivivax Gelatinosus

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Kinetic studies of the oxidation and reduction of Chromatium high potential iron-sulfur protein (HiPIP) by inorganic complexes. Comparison of the electron transfer reactivities of HiPIP and horse heart cytochrome c

Journal of the American Chemical Society ◽

10.1021/ja00424a028 ◽

1976 ◽

Vol 98 (8) ◽

pp. 2177-2180 ◽

Author(s):

Jill Rawlings ◽

Scot Wherland ◽

Harry B. Gray

Keyword(s):

Electron Transfer ◽

Cytochrome C ◽

Kinetic Studies ◽

High Potential ◽

Horse Heart Cytochrome ◽

Iron Sulfur ◽

Inorganic Complexes ◽

Sulfur Protein ◽

Iron Sulfur Protein ◽

Horse Heart Cytochrome C

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Structure, organization and expression of the genes encoding mitochondrial cytochrome c 1 and the Rieske iron-sulfur protein in Chlamydomonas reinhardtii

Molecular Genetics and Genomics ◽

10.1007/s00438-002-0779-x ◽

2003 ◽

Vol 268 (5) ◽

pp. 637-644 ◽

Author(s):

A. Atteia ◽

R. van Lis ◽

D. Wetterskog ◽

E.-B. Gutiérrez-Cirlos ◽

L. Ongay-Larios ◽

...

Keyword(s):

Cytochrome C ◽

Chlamydomonas Reinhardtii ◽

Mitochondrial Cytochrome ◽

Iron Sulfur ◽

Genes Encoding ◽

Sulfur Protein ◽

Iron Sulfur Protein ◽

Rieske Iron Sulfur Protein ◽

Mitochondrial Cytochrome C

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Functional flexibility of electron flow between quinol oxidation Qo site of cytochrome bc1 and cytochrome c revealed by combinatory effects of mutations in cytochrome b, iron-sulfur protein and cytochrome c1

Biochimica et Biophysica Acta (BBA) - Bioenergetics ◽

10.1016/j.bbabio.2018.04.010 ◽

2018 ◽

Vol 1859 (9) ◽

pp. 754-761

Author(s):

Arkadiusz Borek ◽

Robert Ekiert ◽

Artur Osyczka

Keyword(s):

Cytochrome C ◽

Cytochrome B ◽

Electron Flow ◽

Cytochrome Bc1 ◽

Functional Flexibility ◽

Iron Sulfur ◽

Cytochrome C1 ◽

Sulfur Protein ◽

Iron Sulfur Protein ◽

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Study of the high-potential iron sulfur protein in Halorhodospira halophila confirms that it is distinct from cytochrome c as electron carrier

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.0407768102 ◽

2005 ◽

Vol 102 (9) ◽

pp. 3260-3265 ◽

Author(s):

C. Lieutaud ◽

J. Alric ◽

M. Bauzan ◽

W. Nitschke ◽

B. Schoepp-Cothenet

Keyword(s):

Cytochrome C ◽

High Potential ◽

Electron Carrier ◽

Iron Sulfur ◽

Sulfur Protein ◽

Iron Sulfur Protein ◽

Halorhodospira Halophila

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Isolation and reconstitution of the iron-sulfur protein in ubiquinol-cytochrome c oxidoreductase complex. Phospholipids are essential for the integration of the iron-sulfur protein in the complex.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)89855-6 ◽

1984 ◽

Vol 259 (22) ◽

pp. 14059-14063 ◽

Author(s):

Y Shimomura ◽

M Nishikimi ◽

T Ozawa

Keyword(s):

Cytochrome C ◽

Iron Sulfur ◽

Sulfur Protein ◽

Iron Sulfur Protein

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