Spectroscopic Studies of Bacterial Iron-Sulfur Proteins (Electron Paramagnetic Resonance, Magnetic Circular Dichroism).

Content Provider	Semantic Scholar
Author	Bennett, Deborah E.
Copyright Year	1986
Abstract	Iron-sulfur proteins play a vital role in metabolism; mediating such life-sustaining processes as aerobic and anaerobic respiration, nitrogen fixation, and photosynthesis. This work employs low temperature magnetic circular diohroism (MCD), electron paramagnetic resonance (EPR), and UV-visible spectroscopy to characterize the iron-sulfur clusters of the following bacterial proteins: Azotobaoter vinelandii ferredoxinl, Thermus therroophilus ferredoxin, EBSh.PEi.ghift gali nitrate reductase and the rubredoxin and ferredoxin from Clostridium Eftg.fegur.iflQUmNovel [3Fe-xS] clusters were identified in A. vinelandii Fdl, 2L thermophilus Fd, ferricyanide treated C. pasteurianum Fd, and EL. coli nitrate reductase. The uniformity of the magnetic and electronic properties of these clusters in both the oxidized and the reduced states indicates a common iron-sulfur core'structure for this type of cluster. EL coli nitrate reductase is the first example of an active enzyme which contains a [3Fe-xS] cluster. This argues against the currently prevailing hypothesis that all such clusters are isolation artifacts. This work has also developed the potential of low
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Alternate Webpage(s)	https://digitalcommons.lsu.edu/cgi/viewcontent.cgi?article=5172&context=gradschool_disstheses
Language	English
Access Restriction	Open
Content Type	Text
Resource Type	Article