The binding sites of iron in rubredoxin from Micrococcus aerogenes.
- 1 January 1967
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 57 (1) , 122-127
- https://doi.org/10.1073/pnas.57.1.122
Abstract
From the electron paramagnetic resonance (EPR) spectrum and its variation with pH, the sequence studies on the location of cysteine residues and the quantitative analysis of the number of -SH groups, it is suggested that the 1 ferric Fe in rubre-doxin is coordinately bonded in a rhombic symmetry to 4 -SH groups (provided by 4 cysteine residues) and possibly to tyrosine or lysine residues. The cysteine residues are located in positions, 6, 9, 38 and 41 in the rubredoxin molecule. The Fe may function not only as an electron acceptor but to stabilize the conformation of the molecule.This publication has 10 references indexed in Scilit:
- The Amino Acid Sequence of Clostridium pasteurianum Ferredoxin*Biochemistry, 1966
- On the ligand field of iron in ferredoxin from spinach chloroplasts and related nonheme iron enzymes.Proceedings of the National Academy of Sciences, 1966
- On the Magnetic Resonance of Spinach FerredoxinJournal of Biological Chemistry, 1966
- Rubredoxin: a new electron transfer protein from Clostridium pasteurianum.Proceedings of the National Academy of Sciences, 1965
- A Compositional Assay for Insulin Applied to a Search for “Proinsulin”Journal of Biological Chemistry, 1965
- Investigation of the Iron and Copper Complexes of Avian Conalbumins and Human Transferrins by Electron Paramagnetic Resonance*Biochemistry, 1963
- Tryptic cleavage at cysteinyl peptide bondsBiochemical and Biophysical Research Communications, 1963
- The specific binding of iron(III) and copper(II) to transferrin and conalbuminBiochimica et Biophysica Acta, 1963
- FERMENTATION OF AMINO ACIDS BY MICROCOCCUS AEROGENESJournal of Bacteriology, 1957