Biomaterial Database

Identification of a Ni- and Fe-containing cluster in Rhodospirillum rubrum carbon monoxide dehydrogenase. 1989

P J Stephens, and M C McKenna, and S A Ensign, and D Bonam, and P W Ludden

Department of Chemistry, University of Southern California, Los Angeles 90089-0482.

Methyl viologen-oxidized carbon monoxide dehydrogenase (CODH) from Rhodospirillum rubrum exhibits complex EPR. Comparison to EPR of oxidized apo-CODH (CODH from which Ni is lacking) leads to the identification of signals whose intensity is correlated with the presence of Ni. 61Ni labeling observably broadens the sharpest feature of these signals, as does 57Fe. R. rubrum CODH thus contains a cluster containing both Ni and Fe. The EPR associated with this cluster is unlike any EPR previously attributed to Ni-containing prosthetic groups in other CODH enzymes or Ni-containing hydrogenases. The CO-analogue, CN-, perturbs the EPR signals that are attributed to the Ni-Fe species.

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
D009097	Multienzyme Complexes	Systems of enzymes which function sequentially by catalyzing consecutive reactions linked by common metabolic intermediates. They may involve simply a transfer of water molecules or hydrogen atoms and may be associated with large supramolecular structures such as MITOCHONDRIA or RIBOSOMES.	Complexes, Multienzyme
D009532	Nickel	A trace element with the atomic symbol Ni, atomic number 28, and atomic weight 58.69. It is a cofactor of the enzyme UREASE.
D010084	Oxidation-Reduction	A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).	Redox,Oxidation Reduction
D010269	Paraquat	A poisonous dipyridilium compound used as contact herbicide. Contact with concentrated solutions causes irritation of the skin, cracking and shedding of the nails, and delayed healing of cuts and wounds.	Methyl Viologen,Gramoxone,Paragreen A,Viologen, Methyl
D004578	Electron Spin Resonance Spectroscopy	A technique applicable to the wide variety of substances which exhibit paramagnetism because of the magnetic moments of unpaired electrons. The spectra are useful for detection and identification, for determination of electron structure, for study of interactions between molecules, and for measurement of nuclear spins and moments. (From McGraw-Hill Encyclopedia of Science and Technology, 7th edition) Electron nuclear double resonance (ENDOR) spectroscopy is a variant of the technique which can give enhanced resolution. Electron spin resonance analysis can now be used in vivo, including imaging applications such as MAGNETIC RESONANCE IMAGING.	ENDOR,Electron Nuclear Double Resonance,Electron Paramagnetic Resonance,Paramagnetic Resonance,Electron Spin Resonance,Paramagnetic Resonance, Electron,Resonance, Electron Paramagnetic,Resonance, Electron Spin,Resonance, Paramagnetic
D000445	Aldehyde Oxidoreductases	Oxidoreductases that are specific for ALDEHYDES.	Aldehyde Oxidoreductase,Oxidoreductase, Aldehyde,Oxidoreductases, Aldehyde
D001051	Apoenzymes	The protein components of enzyme complexes (HOLOENZYMES). An apoenzyme is the holoenzyme minus any cofactors (ENZYME COFACTORS) or prosthetic groups required for the enzymatic function.	Apoenzyme
D001059	Apoproteins	The protein components of a number of complexes, such as enzymes (APOENZYMES), ferritin (APOFERRITINS), or lipoproteins (APOLIPOPROTEINS).	Apoprotein
D012247	Rhodospirillum rubrum	Vibrio- to spiral-shaped phototrophic bacteria found in stagnant water and mud exposed to light.