| Resonance Raman studies of ETE dehydrogenase (an iron sulfur flavoprotein). | |
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MedLine Citation:
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PMID: 6870891 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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ETF Dehydrogenase is an iron sulfur flavoprotein responsible for the transfer of electrons between electron transfer flavoprotein (ETF) and CoQ of the electron transport chain. We have determined the resonance Raman spectrum of this enzyme observing in the process at least seven of thirteen flavin bands in the 1100cm-1-1600 cm-1 region of the Raman spectrum. The positions of three of these bands, II, IX, and X (see Figure I and Table I for band numbering system) in ETF dehydrogenase is very similar to their positions in aqueous solution of flavins in which water is hydrogen bonded to N-1, N-5, C=0(2), C=0(4), and N-H(3) of flavin. Conversely the positions of the flavin Raman bands are considerably shifted from those of flavin in nonhydrogen bonding solvent. The positions of bands II, IX, and X are nearly identical to those in the flavoprotein glutathione reductase; x-ray structural investigations on this enzyme indicate that there is extensive hydrogen bonding between FAD and protein in this molecule. A previous study in our laboratory has demonstrated that metal complexation at N-5 and C=0(4) with either Ru or Ag produces large shifts in the positions of Raman bands II, VI, IX, and X. None of these shifts are observed in ETF dehydrogenase indicating that there is no direct inner sphere coordination of Fe to flavin. In addition to the Raman bands of flavin observed in our spectrum, we also observe one band that is in the Fe-S stretching region observed for a variety of Fe-S proteins. This band is located at 331 cm-1. The frequency of the band corresponds to the 335 cm-1 band associated with the strongest Fe-S stretching mode in the 4Fe-4S protein ferrodoxin from C. pasterianum. The observed frequency is quite different from that of the 3Fe-3S proteins such as ferrodoxin(II) from D. gigas. Finally, ETF dehydrogenase shows no loss of activity or visual evidence of photodegradation in the laser beam as most other FeS proteins do. |
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Authors:
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J Schmidt; J Beckmann; F Frerman; J T McFarland |
Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S. |
Journal Detail:
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Title: Biochemical and biophysical research communications Volume: 113 ISSN: 0006-291X ISO Abbreviation: Biochem. Biophys. Res. Commun. Publication Date: 1983 Jun |
Date Detail:
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Created Date: 1983-08-11 Completed Date: 1983-08-11 Revised Date: 2008-11-21 |
Medline Journal Info:
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Nlm Unique ID: 0372516 Medline TA: Biochem Biophys Res Commun Country: UNITED STATES |
Other Details:
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Languages: eng Pagination: 784-90 Citation Subset: IM |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Animals Chemical Phenomena Chemistry Electron-Transferring Flavoproteins* Iron-Sulfur Proteins / isolation & purification*, physiology Metalloproteins / isolation & purification* Mitochondria, Liver / enzymology Multienzyme Complexes* Oxidoreductases / classification, isolation & purification* Oxidoreductases Acting on CH-NH Group Donors* Spectrum Analysis, Raman Structure-Activity Relationship Swine |
| Grant Support | |
ID/Acronym/Agency:
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AM15527/AM/NIADDK NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Electron-Transferring Flavoproteins; 0/Iron-Sulfur Proteins; 0/Metalloproteins; 0/Multienzyme Complexes; EC 1.-/Oxidoreductases; EC 1.5.-/Oxidoreductases Acting on CH-NH Group Donors; EC 1.5.5.1/electron-transferring-flavoprotein dehydrogenase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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