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Volumn 96, Issue 7, 1996, Pages 2491-2513

Protein control of redox potentials of iron-sulfur proteins

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EID: 0001531848     PISSN: 00092665     EISSN: None     Source Type: Journal    
DOI: 10.1021/cr950045w     Document Type: Article
Times cited : (303)

References (119)
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    • note
    • There have been quantum mechanical calculations on [Fe-S] clusters; see, for example: Noodleman, L.; Case, D. A. In ref 2; P 425.
  • 23
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    • note
    • It might appear that changes in Δv would more correctly be compared to changes in the redox enthalpy, ΔH, rather than the redox free energy, AG. For reasons discussed at length elsewhere (ref 14) this is not the case.
  • 25
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    • For a comparison of results obtained using eq 9 to the predictions of a more rigorous all-atom solvent model, See: King, G.; Warshel, A. J. Chem. Phys. 1989, 91, 3647.
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    • note
    • 8,9 used a 2 Å inner grid; a 1 Å grid is now preferred.
  • 28
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    • Lovenberg, W., Ed.; Academic Press: New York, Chapter 4
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    • Personal Communication
    • Holden, H. M. Personal Communication, 1996. For the earlier 2.5 Å structure (PDB File 1FXA), see: Rypniewski, W. R.; Breiter, D. R.; Benning, M. M.; Wesenberg, G.; Oh, B. H.; Markley, J. L.; Rayment, I.; Holden, H. M. Biochemistry 1991, 30, 4126.
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  • 54
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    • Personal Communication
    • Holden, H. M. Personal Communication, 1996. For the earlier 2.5 Å structure (PDB File 2HIP) see: Breiter, D. R.; Meyer, T. E.; Payment, I.; Holden, H. M. J. Biol. Chem. 1991, 266, 18660.
    • (1996)
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    • note
    • Trimethyl amine dehydrogenase being the exception to this rule. Redox potentials have been reported from +100 to -40 mV. See ref 97.
  • 114
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    • note
    • 27 It is not known whether this phenomenon occurs in other HiPIPs.
  • 116
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    • note
    • 68


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