109 related articles for article (PubMed ID: 176192)
1. 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.
Rawlings J; Wherland S; Gray HB
J Am Chem Soc; 1976 Apr; 98(8):2177-80. PubMed ID: 176192
[No Abstract] [Full Text] [Related]
2. Oxidation-reduction properties of Chromatium vinosum high potential iron-sulfur protein.
Mizrahi IA; Wood FE; Cusanovich MA
Biochemistry; 1976 Jan; 15(2):343-8. PubMed ID: 2285
[TBL] [Abstract][Full Text] [Related]
3. Electron-transfer protein reactivities. Kinetic studies of the oxidation of horse heart cytochrome c, Chromatium vinosum high potential iron-sulfur protein, Pseudomonas aeruginosa azurin, bean plastocyanin, and Rhus vernicifera stellacyanin by pentaamminepyridineruthenium(III).
Cummins D; Gray HB
J Am Chem Soc; 1977 Jul; 99(15):5158-67. PubMed ID: 194940
[No Abstract] [Full Text] [Related]
4. High-potential iron-sulfur proteins and their possible site of electron transfer.
Aprahamian G; Feinberg BA
Biochemistry; 1981 Feb; 20(4):915-9. PubMed ID: 6260144
[TBL] [Abstract][Full Text] [Related]
5. Kinetics of oxidation and reduction of high-potential iron-sulfur proteins with nonphysiological reactants.
Mizrahi IA; Meyer TE; Cusanovich MA
Biochemistry; 1980 Oct; 19(21):4727-33. PubMed ID: 7426625
[TBL] [Abstract][Full Text] [Related]
6. The role of high-potential iron protein and cytochrome c(8) as alternative electron donors to the reaction center of Chromatium vinosum.
Verméglio A; Li J; Schoepp-Cothenet B; Pratt N; Knaff DB
Biochemistry; 2002 Jul; 41(28):8868-75. PubMed ID: 12102629
[TBL] [Abstract][Full Text] [Related]
7. Electron transfer reactions of high-potential iron-sulfur proteins and c-type cytochromes.
Mizrahi IA; Cusanovich MA
Biochemistry; 1980 Oct; 19(21):4733-7. PubMed ID: 6252957
[TBL] [Abstract][Full Text] [Related]
8. Experimental evidence for the role of buried polar groups in determining the reduction potential of metalloproteins: the S79P variant of Chromatium vinosum HiPIP.
Babini E; Borsari M; Capozzi F; Eltis LD; Luchinat C
J Biol Inorg Chem; 1999 Dec; 4(6):692-700. PubMed ID: 10631600
[TBL] [Abstract][Full Text] [Related]
9. Chromatium flavocytochrome c: kinetics of reduction of the heme subunit, and the flavocytochrome c-mitochondrial cytochrome c complex.
Meyer TE; Vorkink WP; Tollin G; Cusanovich MA
Arch Biochem Biophys; 1985 Jan; 236(1):52-8. PubMed ID: 2981511
[TBL] [Abstract][Full Text] [Related]
10. The role of histidine-42 in the oxidation-reduction mechanism of Chromatium vinosum high potential iron-sulfur protein.
Nettesheim DG; Johnson WV; Feinberg BA
Biochim Biophys Acta; 1980 Dec; 593(2):371-83. PubMed ID: 7236640
[TBL] [Abstract][Full Text] [Related]
11. Kinetics of photooxidation of soluble cytochromes, HiPIP, and azurin by the photosynthetic reaction center of the purple phototrophic bacterium Rhodopseudomonas viridis.
Meyer TE; Bartsch RG; Cusanovich MA; Tollin G
Biochemistry; 1993 May; 32(18):4719-26. PubMed ID: 8387812
[TBL] [Abstract][Full Text] [Related]
12. Dependence of the rates of dissolution of the Fe4S4 clusters of Chromatium vinosum high-potential iron protein and ferredoxin on cluster oxidation state.
Maskiewicz R; Bruice TC
Proc Natl Acad Sci U S A; 1977 Dec; 74(12):5231-4. PubMed ID: 23530
[TBL] [Abstract][Full Text] [Related]
13. Formation of super-reduced Chromatium high-potential iron--sulphur protein in aqueous solution by pulse radiolysis.
Butler J; Sykes AG; Buxton GV; Harrington PC; Wilkins RG
Biochem J; 1980 Sep; 189(3):641-4. PubMed ID: 7213348
[TBL] [Abstract][Full Text] [Related]
14. Isolation and characterization of soluble electron transfer proteins from Chromatium purpuratum.
Kerfeld CA; Chan C; Hirasawa M; Kleis-SanFrancisco S; Yeates TO; Knaff DB
Biochemistry; 1996 Jun; 35(24):7812-8. PubMed ID: 8672482
[TBL] [Abstract][Full Text] [Related]
15. 1H NMR studies of oxidized high-potential iron protein from Chromatium vinosum. Nuclear Overhauser effect measurements.
Cowan JA; Sola M
Biochemistry; 1990 Jun; 29(23):5633-7. PubMed ID: 2386791
[TBL] [Abstract][Full Text] [Related]
16. Cluster characterization in iron-sulfur proteins by magnetic circular dichroism.
Stephens PJ; Thomson AJ; Keiderling TA; Rawlings J; Rao KK; Hall DO
Proc Natl Acad Sci U S A; 1978 Nov; 75(11):5273-5. PubMed ID: 281679
[TBL] [Abstract][Full Text] [Related]
17. The iron electron-nuclear double resonance (ENDOR) of 4-Fe clusters in iron-sulfur proteins from Chromatium and Clostridium pasteurianum.
Anderson RE; Anger G; Petersson L; Ehrenberg A; Cammack R; Hall DO; Mullinger R; Rao KK
Biochim Biophys Acta; 1975 Jan; 376(1):63-71. PubMed ID: 164903
[TBL] [Abstract][Full Text] [Related]
18. Investigation of the role of a surface patch in the self-association of Chromatium vinosum high potential iron-sulfur protein.
Couture MM; Auger M; Rosell F; Mauk AG; Boubour E; Lennox RB; Eltis LD
Biochim Biophys Acta; 1999 Aug; 1433(1-2):159-69. PubMed ID: 10446369
[TBL] [Abstract][Full Text] [Related]
19. Electron transfer from HiPIP to the photooxidized tetraheme cytochrome subunit of Allochromatium vinosum reaction center: new insights from site-directed mutagenesis and computational studies.
Venturoli G; Mamedov MD; Mansy SS; Musiani F; Strocchi M; Francia F; Semenov AY; Cowan JA; Ciurli S
Biochemistry; 2004 Jan; 43(2):437-45. PubMed ID: 14717598
[TBL] [Abstract][Full Text] [Related]
20. Methionine-oxidized horse heart cytochrome c. III. Ascorbate reduction and the methionine-80-sulfur-iron linkage.
Myer YP; Kumar S
J Protein Chem; 1989 Feb; 8(1):33-50. PubMed ID: 2548524
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
