메뉴 건너뛰기




Volumn 126, Issue 17, 2004, Pages 5413-5426

Strategy for the Study of Paramagnetic Proteins with Slow Electronic Relaxation Rates by NMR Spectroscopy: Application to Oxidized Human [2Fe-2S] Ferredoxin

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CARBON; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PARAMAGNETIC MATERIALS; RESONANCE;

EID: 2342512067     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja037077i     Document Type: Article
Times cited : (40)

References (85)
  • 40
    • 2342627856 scopus 로고
    • Morales et al. claim to have reported the structure of reduced Anabaena Fd; however, they admit that their sample was a mixture of oxidized and reduced and offer no evidence to quantitate the amounts. Notably, the bond Fe-S bond lengths they report do not change upon reduction. Thus, their structure cannot rightly be considered to be that of a reduced Fd. EXAFS studies of [2Fe-2S] Fds have shown increases in both the Fe-Fe and average Fe-S distances upon reduction (Teo, B.-T.; Shulman, R. G.; Brown, G. S., Meixner, A. E. J. Am. Chem. Soc. 1979, 101, 5642-5631, and Cosper, N. J.; Cosper, M. M.; Johnson, M. L.; Iwasaki, T.; Meyer, J.; Scott, R. A. J. Inorg. Biochem. 2001, 86, 187); however, it is not possible to ascertain what impact that might have on the structure of the rest of the protein.
    • (1979) J. Am. Chem. Soc. , vol.101 , pp. 5642-5631
    • Teo, B.-T.1    Shulman, R.G.2    Brown, G.S.3    Meixner, A.E.4
  • 41
    • 2342583984 scopus 로고    scopus 로고
    • Morales et al. claim to have reported the structure of reduced Anabaena Fd; however, they admit that their sample was a mixture of oxidized and reduced and offer no evidence to quantitate the amounts. Notably, the bond Fe-S bond lengths they report do not change upon reduction. Thus, their structure cannot rightly be considered to be that of a reduced Fd. EXAFS studies of [2Fe-2S] Fds have shown increases in both the Fe-Fe and average Fe-S distances upon reduction (Teo, B.-T.; Shulman, R. G.; Brown, G. S., Meixner, A. E. J. Am. Chem. Soc. 1979, 101, 5642-5631, and Cosper, N. J.; Cosper, M. M.; Johnson, M. L.; Iwasaki, T.; Meyer, J.; Scott, R. A. J. Inorg. Biochem. 2001, 86, 187); however, it is not possible to ascertain what impact that might have on the structure of the rest of the protein.
    • (2001) J. Inorg. Biochem. , vol.86 , pp. 187
    • Cosper, N.J.1    Cosper, M.M.2    Johnson, M.L.3    Iwasaki, T.4    Meyer, J.5    Scott, R.A.6
  • 68
    • 2342591897 scopus 로고    scopus 로고
    • www.bmrb.wisc.edu.
  • 70
    • 2342447861 scopus 로고    scopus 로고
    • www.cgl.ucsf.edu/home/sparky.
  • 78
    • 2342510839 scopus 로고    scopus 로고
    • note
    • Extensive assignments have been made before for paramagnetic proteins with faster electronic relaxation, such as heme and [4Fe-4S] cluster proteins.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.