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Volumn 122, Issue 20, 2000, Pages 4926-4936

Mossbauer study of the MoFe protein of nitrogenase from Azotobacter vinelandii using selective 57Fe enrichment of the M-centers

Author keywords

[No Author keywords available]

Indexed keywords

IRON; MOLYBDENUM; NITROGENASE; PROTEIN;

EID: 0001179260     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja000254k     Document Type: Article
Times cited : (148)

References (74)
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    • note
    • In cases with superb resolution, such as that observed for the spectra of E. coli sulfite reductase, we found that the absorption of the siroheme iron and the [4Fe-4S] cluster were exactly in a 1:4 ratio. The spectra of reduced [3Fe-4S] clusters provide additional support for this assumption.
  • 35
    • 0343228260 scopus 로고    scopus 로고
    • note
    • eff|, the quantity determining the magnetic splitting, increases at low field and decreases at high field. This pattern of increasing and decreasing splittings is orientation- and field-dependent, and since the A values are small, outward and inward moving features are not resolved at all. However, the splitting pattern is still easily distinguished from that resulting from a site with positive A values; for the latter, the magnetic splittings will always increase with increasing applied field.
  • 36
    • 0342793705 scopus 로고    scopus 로고
    • Footnote 21 of ref 20
    • Footnote 21 of ref 20.
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    • 0009746605 scopus 로고
    • Cammack, R., Ed.; Academic Press: New York
    • Holm, R. H. In Advances in Inorganic Chemistry; Cammack, R., Ed.; Academic Press: New York, 1992; Vol. 38, pp 1-62.
    • (1992) Advances in Inorganic Chemistry , vol.38 , pp. 1-62
    • Holm, R.H.1
  • 42
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    • note
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  • 51
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    • personal communication
    • Trautwein, A. X., personal communication. Krahn, E.; Weiss, B. J. R.; Kroeckel, M.; Groppe, J.; Henkel, G.; Cramer, S. P.; Trautwein, A. X.; Schneider, K.; Mueller, A. J. Biol. Inorg. Chem., submitted.
    • Trautwein, A.X.1
  • 62
    • 0342358697 scopus 로고    scopus 로고
    • note
    • 54 have shown that extracted cofactor is negatively charged. If three negative charges are assigned to homocitrate and if one assumes that a negatively charged ion replaces the thiolate sulfur of αCys 275, the extracted cofactor will be negatively charged in the S = 3/2 state regardless of whether six or four Fe sites are ferrous.
  • 67
    • 0343228248 scopus 로고    scopus 로고
    • note
    • R) state and that 20% will be split among more reduced states of the MoFe protein. Our analysis suggests that ca. 60% of the FeMoco sites are one-electron reduced.
  • 68
    • 0342793697 scopus 로고    scopus 로고
    • note
    • av spread over seven iron sites corresponds to a change of 0.42 mm/s, i.e., roughly to about one electron.
  • 70
    • 0343228242 scopus 로고    scopus 로고
    • note
    • eff is sufficiently larger than the zero-field splittings.
  • 72
    • 0343228243 scopus 로고    scopus 로고
    • note
    • I is related to reduced FeMo cofactor.
  • 74
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    • note
    • 3+.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.