BIOMAT Database Logo BIOMAT Database Logo

Iron K-edge X-ray absorption spectroscopy of the iron-molybdenum cofactor of nitrogenase from Klebsiella pneumoniae. 1988

J M Arber, and A C Flood, and C D Garner, and C A Gormal, and S S Hasnain, and B E Smith
Department of Chemistry, University of Manchester, U.K.

Iron K-edge X-ray absorption data for the iron-molybdenum cofactor ('FeMoco') from Klebsiella pneumoniae reported here provide the first evidence for long-range structural order in the cofactor [Fe...Fe(Mo) = 0.368 nm in addition to Fe...S = 0.22 nm and Fe...Fe(Mo) = 0.27 nm] and, in contrast with previously published data [Antonio, Teo, Orme-Johnson, Nelson, Groh, Lindahl, Kauzlarich & Averill (1982) J. Am. Chem. Soc. 104, 4703-4705], indicate that most of the iron centres are not co-ordinated to light (oxygen, nitrogen) atoms. This demonstrates that presently available chemical models for FeMoco are inadequate.

UI MeSH Term Description Entries
D007501 Iron A metallic element with atomic symbol Fe, atomic number 26, and atomic weight 55.85. It is an essential constituent of HEMOGLOBINS; CYTOCHROMES; and IRON-BINDING PROTEINS. It plays a role in cellular redox reactions and in the transport of OXYGEN. Iron-56,Iron 56
D007711 Klebsiella pneumoniae Gram-negative, non-motile, capsulated, gas-producing rods found widely in nature and associated with urinary and respiratory infections in humans. Bacillus pneumoniae,Bacterium pneumoniae crouposae,Hyalococcus pneumoniae,Klebsiella pneumoniae aerogenes,Klebsiella rhinoscleromatis
D008983 Molybdoferredoxin A non-heme iron-sulfur protein isolated from Clostridium pasteurianum and other bacteria. It is a component of NITROGENASE, which is active in nitrogen fixation, and consists of two subunits with molecular weights of 59.5 kDa and 50.7 kDa, respectively. Molybdenum-Iron Protein,FeMo Cofactor,Iron-Molybdenum Cofactor,MoFe Protein,Iron Molybdenum Cofactor,Molybdenum Iron Protein
D009591 Nitrogenase An enzyme system that catalyzes the fixing of nitrogen in soil bacteria and blue-green algae (CYANOBACTERIA). EC 1.18.6.1. Dinitrogenase,Vanadium Nitrogenase,Nitrogenase, Vanadium
D005288 Ferredoxins Iron-containing proteins that transfer electrons, usually at a low potential, to flavoproteins; the iron is not present as in heme. (McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed) Ferredoxin,Ferredoxin I,Ferredoxin II,Ferredoxin III
D013057 Spectrum Analysis The measurement of the amplitude of the components of a complex waveform throughout the frequency range of the waveform. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed) Spectroscopy,Analysis, Spectrum,Spectrometry
D014965 X-Rays Penetrating electromagnetic radiation emitted when the inner orbital electrons of an atom are excited and release radiant energy. X-ray wavelengths range from 1 pm to 10 nm. Hard X-rays are the higher energy, shorter wavelength X-rays. Soft x-rays or Grenz rays are less energetic and longer in wavelength. The short wavelength end of the X-ray spectrum overlaps the GAMMA RAYS wavelength range. The distinction between gamma rays and X-rays is based on their radiation source. Grenz Ray,Grenz Rays,Roentgen Ray,Roentgen Rays,X Ray,X-Ray,Xray,Radiation, X,X-Radiation,Xrays,Ray, Grenz,Ray, Roentgen,Ray, X,Rays, Grenz,Rays, Roentgen,Rays, X,X Radiation,X Rays,X-Radiations

Related Publications

J M Arber, and A C Flood, and C D Garner, and C A Gormal, and S S Hasnain, and B E Smith
Iron K-edge X-ray-absorption spectroscopy of the iron-vanadium cofactor of the vanadium nitrogenase from Azotobacter chroococcum.
March 1990, The Biochemical journal,
J M Arber, and A C Flood, and C D Garner, and C A Gormal, and S S Hasnain, and B E Smith
X-ray emission spectroscopy evidences a central carbon in the nitrogenase iron-molybdenum cofactor.
November 2011, Science (New York, N.Y.),
J M Arber, and A C Flood, and C D Garner, and C A Gormal, and S S Hasnain, and B E Smith
Comparison of iron-molybdenum cofactor-deficient nitrogenase MoFe proteins by X-ray absorption spectroscopy: implications for P-cluster biosynthesis.
July 2004, The Journal of biological chemistry,
J M Arber, and A C Flood, and C D Garner, and C A Gormal, and S S Hasnain, and B E Smith
Nitrogenase from nifV mutants of Klebsiella pneumoniae contains an altered form of the iron-molybdenum cofactor.
January 1984, The Biochemical journal,
J M Arber, and A C Flood, and C D Garner, and C A Gormal, and S S Hasnain, and B E Smith
Selenol binds to iron in nitrogenase iron-molybdenum cofactor: an extended x-ray absorption fine structure study.
February 1994, Proceedings of the National Academy of Sciences of the United States of America,
J M Arber, and A C Flood, and C D Garner, and C A Gormal, and S S Hasnain, and B E Smith
Letter: Molybdenum X-ray absorption edge spectra. The chemical state of molybdenum in nitrogenase.
March 1976, Journal of the American Chemical Society,
J M Arber, and A C Flood, and C D Garner, and C A Gormal, and S S Hasnain, and B E Smith
Low-temperature magnetic-circular-dichroism spectroscopy of the iron-molybdenum cofactor and the complementary cofactor-less MoFe protein of Klebsiella pneumoniae nitrogenase.
April 1984, The Biochemical journal,
J M Arber, and A C Flood, and C D Garner, and C A Gormal, and S S Hasnain, and B E Smith
Small-angle x-ray scattering studies of the iron-molybdenum cofactor from Azotobacter vinelandii nitrogenase.
October 1993, The Journal of biological chemistry,
J M Arber, and A C Flood, and C D Garner, and C A Gormal, and S S Hasnain, and B E Smith
Isolation of an iron-molybdenum cofactor from nitrogenase.
August 1977, Proceedings of the National Academy of Sciences of the United States of America,
J M Arber, and A C Flood, and C D Garner, and C A Gormal, and S S Hasnain, and B E Smith
Localized Electronic Structure of Nitrogenase FeMoco Revealed by Selenium K-Edge High Resolution X-ray Absorption Spectroscopy.
August 2019, Journal of the American Chemical Society,
Copied contents to your clipboard!