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Volumn 318, Issue 5855, 2007, Pages 1464-1468

Solvent tuning of electrochemical potentials in the active sites of HiPIP versus ferredoxin

Author keywords

[No Author keywords available]

Indexed keywords

FERREDOXIN; IRON SULFUR PROTEIN;

EID: 36749090019     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1147753     Document Type: Article
Times cited : (184)

References (46)
  • 1
    • 84912414819 scopus 로고
    • Iron-Sulfur Proteins
    • T. G. Spiro, Ed, of, Wiley, New York
    • T. G. Spiro, Ed., Iron-Sulfur Proteins, vol. IV of Metal Ions in Biology (Wiley, New York, 1982).
    • (1982) Metal Ions in Biology , vol.4
  • 4
    • 0000430313 scopus 로고    scopus 로고
    • A. Messerschmidt, R. Huber, T. L. Poulos, K. Wieghardt, Eds, Wiley, New York
    • K. Fukuyama, in Handbook of Metalloproteins, A. Messerschmidt, R. Huber, T. L. Poulos, K. Wieghardt, Eds. (Wiley, New York, 2004), p. 543.
    • (2004) Handbook of Metalloproteins , pp. 543
    • Fukuyama, K.1
  • 5
    • 36749032490 scopus 로고    scopus 로고
    • One ferredoxin has been reported to have a potential of -650 mV (6).
    • One ferredoxin has been reported to have a potential of -650 mV (6).
  • 9
    • 36749002346 scopus 로고    scopus 로고
    • All potentials in this report are referenced relative to the normal hydrogen electrode NHE
    • All potentials in this report are referenced relative to the normal hydrogen electrode (NHE).
  • 31
    • 36749011541 scopus 로고    scopus 로고
    • Detailed materials and methods are available on Science Online.
    • Detailed materials and methods are available on Science Online.
  • 35
    • 36749073609 scopus 로고    scopus 로고
    • The [Fe4S4] Fd from Pf is coordinated by an aspartate (Asp14) residue at one Fe. Thus, an Asp14 → Cys14 mutant, which has been characterized to have four cysteines coordinating the four Fe atoms of the cluster, has been used for this study
    • 14 mutant, which has been characterized to have four cysteines coordinating the four Fe atoms of the cluster, has been used for this study.
  • 46
    • 36749021865 scopus 로고    scopus 로고
    • This research was supported by NSF grants CHE-0446304 (E.I.S, RR-01209 (K.O.H, and GM 60329 (M.W.W.A, A.D. received an Evelyn McBain Fellowship from Stanford University. SSRL operations are supported by the U.S. Department of Energy, Office of Basic Energy Sciences. The SSRL Structural Molecular Biology Program is supported by the NIH, National Center for Research Resources, Biomedical Technology Program and by the U.S. Department of Energy, Office of Biological and Environmental Research. The project described was supported by grant number P41 RR-001209 from the National Center for Research Resources NCRR, a component of the NIH, and its contents are solely the responsibility of the authors and do not necessarily represent the official view of NCRR or NIH. J. Brauman is acknowledged for suggestions on the manuscript
    • This research was supported by NSF grants CHE-0446304 (E.I.S.), RR-01209 (K.O.H.), and GM 60329 (M.W.W.A.). A.D. received an Evelyn McBain Fellowship from Stanford University. SSRL operations are supported by the U.S. Department of Energy, Office of Basic Energy Sciences. The SSRL Structural Molecular Biology Program is supported by the NIH, National Center for Research Resources, Biomedical Technology Program and by the U.S. Department of Energy, Office of Biological and Environmental Research. The project described was supported by grant number P41 RR-001209 from the National Center for Research Resources (NCRR), a component of the NIH, and its contents are solely the responsibility of the authors and do not necessarily represent the official view of NCRR or NIH. J. Brauman is acknowledged for suggestions on the manuscript.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.