Infrared Studies on the Interaction of Carbon Monoxide with Divalent Nickel in Hydrogenase from Chromatium vinosum
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چکیده
منابع مشابه
Infrared studies on the interaction of carbon monoxide with divalent nickel in hydrogenase from Chromatium vinosum.
Infrared spectra of a carbon monoxy-bound form of the EPR silent Ni(II) species of hydrogenase isolated from Chromatium vinosum are presented. These spectra show a band at 2060 cm-1 due to v(CO) for a metal-CO complex. This absorbance shifts to 2017 cm-1 upon exposure of the enzyme to 13CO. This band is attributed to v(CO) from a Ni(II)-CO species. It is shown that the CO on this species is pho...
متن کاملThe use of electron-paramagnetic-resonance spectroscopy to establish the properties of nickel and the iron-sulphur cluster in hydrogenase from Chromatium vinosum.
Hydrogenase [hydrogenase: (acceptor) oxidoreductase, EC 1.12. . -1 is present in many bacteria. It is one of the enzymes having potential use in the biophotolysis of water (Weaver et al.. 1980). When we began our research on hydrogenase in 1977, two types of enzymes were known: (i) enzymes containing 12 Fe atoms and an equivalent amount of acid-labile S atoms and (ii) enzymes containing only fo...
متن کاملPal-Like Protein Present in Chromatium vinosum
PAL is a peptidoglycan-associated lipoprotein found in the cell membranes of many Gramnegative bacteria. The presence of PAL has been demonstrated in Escherichia coli and many bacteria. In this paper, we show the presence of a gene coding for a PAL-like protein in C. vinosum, a photosynthetic bacteria and the partial sequence of the PAL gene.
متن کاملStructural examination of the nickel site in chromatium vinosum hydrogenase: redox state oscillations and structural changes accompanying reductive activation and CO binding.
An X-ray absorption spectroscopic study of structural changes occurring at the Ni site of Chromatium vinosum hydrogenase during reductive activation, CO binding, and photolysis is presented. Structural details of the Ni sites for the ready silent intermediate state, SI(r), and the carbon monoxide complex, SI-CO, are presented for the first time in any hydrogenase. Analysis of nickel K-edge ener...
متن کاملBiological and physicochemical properties of the lipopolysaccharide of Chromatium vinosum.
The lipopolysaccharide (LPS) of Chromatium vinosum has anticomplementary activity. This anticomplementary activity is destroyed by alkaline digestion of the LPS and is suppressed by both Mg2+ and Ca2+ ions. Treatment of the LPS with ethylenediaminetetraacetic acid, sodium deoxycholate, or dimethyl sulfoxide did not affect its toxicity toward mice; however, alkaline-treated LPS was not toxic. Tr...
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ژورنال
عنوان ژورنال: Biochemistry
سال: 1994
ISSN: 0006-2960,1520-4995
DOI: 10.1021/bi00197a026