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Indolepyruvate ferredoxin oxidoreductase: An oxygen-sensitive iron–sulfur enzyme from the hyperthermophilic archaeon Thermococcus profundus

Paper ID Volume ID Publish Year Pages File Format Full-Text
20677 43186 2012 5 PDF Available
Title
Indolepyruvate ferredoxin oxidoreductase: An oxygen-sensitive iron–sulfur enzyme from the hyperthermophilic archaeon Thermococcus profundus
Abstract

Thermococcus profundus is a strictly anaerobic sulfur-dependent archaeon that grows optimally at 80°C by peptide fermentation. Indolepyruvate ferredoxin oxidoreductase (IOR), an enzyme involved in the peptide fermentation pathway, was purified to homogeneity from the archaeon under strictly anaerobic conditions. The maximal activity was obtained above the boiling temperature of water (105°C), with a half-life of 62 min at 100°C and 20 min at 105°C. IOR was oxygen-sensitive with a half-life of 7 h at 25°C under aerobic conditions. The specific activity of T. profundus IOR was found to be dependent on the number of [4Fe–4S] clusters in the enzyme.

Keywords
DTT, dithiothreitol; DT, sodium dithionite; IOR, indolepyruvate oxidoreductase; KGOR (OGOR), 2-ketoglutarate ferredoxin oxidoreductase (2-oxoglutarate ferredoxin oxidoreductase); PFOR/POR, pyruvate ferredoxin oxidoreductase; RR, resonance Raman; TPP, thia
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Indolepyruvate ferredoxin oxidoreductase: An oxygen-sensitive iron–sulfur enzyme from the hyperthermophilic archaeon Thermococcus profundus
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Bioscience and Bioengineering - Volume 114, Issue 1, July 2012, Pages 23–27
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us