+ Site Statistics
References:
52,654,530
Abstracts:
29,560,856
PMIDs:
28,072,755
+ Search Articles
+ Subscribe to Site Feeds
Most Shared
PDF Full Text
+ PDF Full Text
Request PDF Full Text
+ Follow Us
Follow on Facebook
Follow on Twitter
Follow on LinkedIn
+ Translate
+ Recently Requested

Structural insights from the molybdenum k edge x ray absorption near edge structure of the iron molybdenum protein of nitrogenase and its iron molybdenum cofactor by comparison with synthetic iron molybdenum sulfur clusters



Structural insights from the molybdenum k edge x ray absorption near edge structure of the iron molybdenum protein of nitrogenase and its iron molybdenum cofactor by comparison with synthetic iron molybdenum sulfur clusters



Journal of the American Chemical Society 107(26): 7935-7940



The Mo environment in the Fe-Mo-S cluster of nitrogenase has been examined by comparison of the Mo K-edge X-ray absorption edge and near edge structure (collectively referred to herein as XANES) of Clostridium pasteurianum and Azotobacter vinelandii FeMo protein, as isolated FeMo cofactor (FeMoco), benzene thiol- and selenol-treated FeMoco, and a variety of synthetic Mo-S complexes and Fe-Mo-S clusters of known structure. There is a distinct correlation between the shapes of the absorption edge features (examined as second derivative absorbance curves) of the synthetic compounds and the environment of the nearest-neighbor atoms around the Mo atom. The significance of these results pertaining to the general problem of the interpretation of XANES spectra is discussed. The Mo XANES of the nitrogenase samples are quite similar to each other and to the XANES of cubane-type MoFe3S4 clusters possessing a MoS3O3 coordination unit. They are dissimilar to the XANES of all other types of synthetic compounds examined. The conclusion from these XANES studies is that the Mo site of the native cluster is approached in these synthetic clusters. This result is complementary to and consistent with, but independent of, results from Mo EXAFS studies.

(PDF emailed within 1 workday: $29.90)

Accession: 006491413

Download citation: RISBibTeXText


Related references

New structural insights into the iron molybdenum cofactor from azotobacter vinelandii nitrogenase through sulfur k and molybdenum l x ray absorption edge studies. Journal of the American Chemical Society 110(12): 3798-3805, 1988

Recent structure determinations of the molybdenum-iron protein of nitrogenase: impact on design of synthetic analogs for the iron-molybdenum-sulfur active site and the iron-molybdenum cofactor. ACS symposium series: 35) 304-331, 1993

Molybdenum k edge extended x ray absorption fine structure studies of synthetic molybdenum iron sulfur clusters containing the tetra thio molybdenum unit development of a fine adjustment technique based on models. Journal of the American Chemical Society 105(12): 3752-3762, 1983

Elicitation of thiomolybdates from the iron molybdenum cofactor of nitrogenase comparison with synthetic iron molybdenum sulfur complexes. European Journal of Biochemistry 159(1): 111-116, 1986

The molybdenum site of nitrogenase part 2 a comparative study of molybdenum iron proteins and the iron molybdenum cofactor by x ray absorption spectroscopy. Journal of the American Chemical Society 100(12): 3814-3819, 1978

Structure of iron ii molybdenum cofactor from azotobacter iron ii molybdenum protein disposition of macro molecules of iron ii molybdenum protein and amino acid analysis. Izvestiya Akademii Nauk SSSR Seriya Biologicheskaya (2): 316-318, 1981

Structural studies of the molybdenum site in the molybdenum iron protein and its iron molybdenum cofactor by exafs. Journal of the American Chemical Society 109(24): 7507-7515, 1987

In vitro synthesis of the iron-molybdenum cofactor of nitrogenase from iron, sulfur, molybdenum, and homocitrate using purified proteins. Proceedings of the National Academy of Sciences of the United States of America 104(45): 17626-17631, 2007

Iron K-edge X-ray absorption spectroscopy of the iron-molybdenum cofactor of nitrogenase from Klebsiella pneumoniae. Biochemical Journal 252(2): 421-425, 1988

Low temperature magnetic circular dichroism spectroscopy of the iron molybdenum cofactor and the complementary cofactor less molybdenum iron protein of klebsiella pneumoniae nitrogenase. Biochemical Journal 219(2): 495-504, 1984

Reconstitution of a partially purified apo molybdenum iron protein of nitrogenase with iron molybdenum cofactor involves the iron protein magnesium atp complex. Abstracts of the Annual Meeting of the American Society for Microbiology 89: 266, 1989

Metal clusters in nitrogenase iron molybdenum protein from azotobacter vinelandii iii. the relationships between the iron content and catalytic activity spectroscopic characteristics of iron molybdenum protein treated with o phenanthroline. Weishengwu Xuebao 29(1): 51-57, 1989

Synthesis and characterization of a new iron molybdenum sulfur cluster containing the hexathiodimolybdenumhexairon 3+ core a precursor to a possible structural analog for the iron molybdenum site of nitrogenase. Journal of the American Chemical Society 107(17): 5005-5006, 1985

Alterations in the alpha subunit of the nitrogenase molybdenum iron protein at amino acid residues 191 and 195 define a domain that changes the catalytic properties of iron molybdenum cofactor. Gresshoff, P M , Et Al (Ed ) Nitrogen Fixation: Achievements And Objectives; 8th International Congress on Nitrogen Fixation, Knoxville, Tennessee, Usa, May 20-26, Xix+869p Routledge, Chapman And Hall: New York, New York, Usa; London, England, Uk Illus 169, 1990

Studies on the iron molybdenum cofactor from the nitrogenase molybdenum iron protein of klebsiella pneumoniae. Newton, W E And S Otsuka (Ed ) Molybdenum Chemistry Of Biological Significance; International Symposium, Lake Biwa, Japan, Apr 10-13, 1979 Ix+425p Plenum Press: New York, N Y , Usa: London, England Illus P179-190, 1980