129 related articles for article (PubMed ID: 11129002)
1. Redox thermodynamics of low-potential iron-sulfur proteins.
Battistuzzi G; D'Onofrio M; Borsari M; Sola M; Macedo AL; Moura JJ; Rodrigues P
J Biol Inorg Chem; 2000 Dec; 5(6):748-60. PubMed ID: 11129002
[TBL] [Abstract][Full Text] [Related]
2. Enthalpy/entropy compensation phenomena in the reduction thermodynamics of electron transport metalloproteins.
Battistuzzi G; Borsari M; Di Rocco G; Ranieri A; Sola M
J Biol Inorg Chem; 2004 Jan; 9(1):23-6. PubMed ID: 14586786
[TBL] [Abstract][Full Text] [Related]
3. Structural origins of redox potentials in Fe-S proteins: electrostatic potentials of crystal structures.
Swartz PD; Beck BW; Ichiye T
Biophys J; 1996 Dec; 71(6):2958-69. PubMed ID: 8968568
[TBL] [Abstract][Full Text] [Related]
4. Influence of charge and polarity on the redox potentials of high-potential iron-sulfur proteins: evidence for the existence of two groups.
Heering HA; Bulsink BM; Hagen WR; Meyer TE
Biochemistry; 1995 Nov; 34(45):14675-86. PubMed ID: 7578075
[TBL] [Abstract][Full Text] [Related]
5. Calculating standard reduction potentials of [4Fe-4S] proteins.
Perrin BS; Niu S; Ichiye T
J Comput Chem; 2013 Mar; 34(7):576-82. PubMed ID: 23115132
[TBL] [Abstract][Full Text] [Related]
6. Density functional and reduction potential calculations of Fe4S4 clusters.
Torres RA; Lovell T; Noodleman L; Case DA
J Am Chem Soc; 2003 Feb; 125(7):1923-36. PubMed ID: 12580620
[TBL] [Abstract][Full Text] [Related]
7. Control of metalloprotein reduction potential: compensation phenomena in the reduction thermodynamics of blue copper proteins.
Battistuzzi G; Bellei M; Borsari M; Canters GW; de Waal E; Jeuken LJ; Ranieri A; Sola M
Biochemistry; 2003 Aug; 42(30):9214-20. PubMed ID: 12885256
[TBL] [Abstract][Full Text] [Related]
8. Spectroscopic characterization of a novel tetranuclear Fe cluster in an iron-sulfur protein isolated from Desulfovibrio desulfuricans.
Tavares P; Pereira AS; Krebs C; Ravi N; Moura JJ; Moura I; Huynh BH
Biochemistry; 1998 Mar; 37(9):2830-42. PubMed ID: 9485434
[TBL] [Abstract][Full Text] [Related]
9. Studies of the redox properties of CDP-6-deoxy-L-threo-D-glycero-4-hexulose-3-dehydrase (E1) and CDP-6-deoxy-L-threo-D-glycero-4-hexulose-3-dehydrase reductase (E3): two important enzymes involved in the biosynthesis of ascarylose.
Burns KD; Pieper PA; Liu HW; Stankovich MT
Biochemistry; 1996 Jun; 35(24):7879-89. PubMed ID: 8672489
[TBL] [Abstract][Full Text] [Related]
10. Factors influencing redox thermodynamics and electron self-exchange for the [Fe4S4] cluster in Chromatium vinosum high potential iron protein: the role of core aromatic residues in defining cluster redox chemistry.
Soriano A; Li D; Bian S; Agarwal A; Cowan JA
Biochemistry; 1996 Sep; 35(38):12479-86. PubMed ID: 8823183
[TBL] [Abstract][Full Text] [Related]
11. Desulfovibrio Gigas hydrogenase: redox properties of the nickel and iron-sulfur centers.
Teixeira M; Moura I; Xavier AV; Dervartanian DV; Legall J; Peck HD; Huynh BH; Moura JJ
Eur J Biochem; 1983 Feb; 130(3):481-4. PubMed ID: 6297907
[TBL] [Abstract][Full Text] [Related]
12. Physicochemical aspects of the movement of the rieske iron sulfur protein during quinol oxidation by the bc(1) complex from mitochondria and photosynthetic bacteria.
Crofts AR; Hong S; Zhang Z; Berry EA
Biochemistry; 1999 Nov; 38(48):15827-39. PubMed ID: 10625447
[TBL] [Abstract][Full Text] [Related]
13. De Novo Design of Iron-Sulfur Proteins.
Dizicheh ZB; Halloran N; Asma W; Ghirlanda G
Methods Enzymol; 2017; 595():33-53. PubMed ID: 28882205
[TBL] [Abstract][Full Text] [Related]
14. Mixed valent sites in biological electron transfer.
Solomon EI; Xie X; Dey A
Chem Soc Rev; 2008 Apr; 37(4):623-38. PubMed ID: 18362972
[TBL] [Abstract][Full Text] [Related]
15. Electron transfer in biological systems: an overview.
Dreyer JL
Experientia; 1984 Jul; 40(7):653-75. PubMed ID: 6378653
[No Abstract] [Full Text] [Related]
16. Redox pathways in electron-transfer proteins: correlations between reactivities, solvent exposure, and unpaired-spin-density distributions.
Tollin G; Hanson LK; Caffrey M; Meyer TE; Cusanovich MA
Proc Natl Acad Sci U S A; 1986 Jun; 83(11):3693-7. PubMed ID: 3012528
[TBL] [Abstract][Full Text] [Related]
17. The type I/type II cytochrome c3 complex: an electron transfer link in the hydrogen-sulfate reduction pathway.
Pieulle L; Morelli X; Gallice P; Lojou E; Barbier P; Czjzek M; Bianco P; Guerlesquin F; Hatchikian EC
J Mol Biol; 2005 Nov; 354(1):73-90. PubMed ID: 16226767
[TBL] [Abstract][Full Text] [Related]
18. EPR and redox characterization of iron-sulfur centers in nitrate reductases A and Z from Escherichia coli. Evidence for a high-potential and a low-potential class and their relevance in the electron-transfer mechanism.
Guigliarelli B; Asso M; More C; Augier V; Blasco F; Pommier J; Giordano G; Bertrand P
Eur J Biochem; 1992 Jul; 207(1):61-8. PubMed ID: 1321049
[TBL] [Abstract][Full Text] [Related]
19. Characterization of the flavins and the iron-sulfur centers of glutamate synthase from Azospirillum brasilense by absorption, circular dichroism, and electron paramagnetic resonance spectroscopies.
Vanoni MA; Edmondson DE; Zanetti G; Curti B
Biochemistry; 1992 May; 31(19):4613-23. PubMed ID: 1316154
[TBL] [Abstract][Full Text] [Related]
20. Modeling the active sites in metalloenzymes. 3. Density functional calculations on models for [Fe]-hydrogenase: structures and vibrational frequencies of the observed redox forms and the reaction mechanism at the Diiron Active Center.
Cao Z; Hall MB
J Am Chem Soc; 2001 Apr; 123(16):3734-42. PubMed ID: 11457105
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
