A variable-temperature direct electrochemical study of metalloproteins from hyperthermophilic microorganisms involves in hydrogen production from pyruvate
Abstract
The hyperthomophilic bacterium Thermotoga maritima and the hyperthermolic archaeon Pyrococcus furiosus grow optimally at 80{degrees} and 100{degrees}C, respectively, by the fermentation of carbohydrates to organic acids, CO{sub 2}, and H{sub 2}. Pyruvate is a major source of reductant for H{sub 2} production during fermentation, and pyruvate ferredoxin oxidoreductase (POR), a 4Fe-type ferredoxin, and hydrogenase have been previously purified from both species. P. furiosus utilizes copper-iron-containing POR and a nickel-iron-containing hydrogenase, whereas the POR of T. maritima lacks copper and its hydrogenase lacks nickel. For all four enzymes and for the two ferredoxins, we have determined their reproduction potentials (E{degrees}` and, where possible, thermodynamic parameters associated with electron transfer {Delta}S{degrees} and {Delta}H{degrees}), using differential pulse voltammetry at temperatures ranging from 25 to 95{degrees}C. 55 refs., 7 fig., 2 tabs.
- Authors:
-
- Univ. of Georgia, Athens, GA (United States)
- Publication Date:
- Sponsoring Org.:
- USDOE
- OSTI Identifier:
- 526065
- Resource Type:
- Journal Article
- Journal Name:
- Biochemistry (Eaton)
- Additional Journal Information:
- Journal Volume: 34; Journal Issue: 21; Other Information: PBD: 30 May 1995
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 55 BIOLOGY AND MEDICINE, BASIC STUDIES; FERREDOXIN; REDUCTION; ENZYME ACTIVITY; OXIDOREDUCTASES; HYDROGENASES; ELECTRON TRANSFER; FERMENTATION; METALLOPROTEINS; IRON; NICKEL; ORGANIC ACIDS; RUBREDOXIN; TEMPERATURE DEPENDENCE; THERMOPHILIC CONDITIONS; METABOLISM; PYRUVIC ACID
Citation Formats
Smith, E T, Blamey, J, Zhou, Z Z, and Adams, M W.W. A variable-temperature direct electrochemical study of metalloproteins from hyperthermophilic microorganisms involves in hydrogen production from pyruvate. United States: N. p., 1995.
Web. doi:10.1021/bi00021a030.
Smith, E T, Blamey, J, Zhou, Z Z, & Adams, M W.W. A variable-temperature direct electrochemical study of metalloproteins from hyperthermophilic microorganisms involves in hydrogen production from pyruvate. United States. https://doi.org/10.1021/bi00021a030
Smith, E T, Blamey, J, Zhou, Z Z, and Adams, M W.W. 1995.
"A variable-temperature direct electrochemical study of metalloproteins from hyperthermophilic microorganisms involves in hydrogen production from pyruvate". United States. https://doi.org/10.1021/bi00021a030.
@article{osti_526065,
title = {A variable-temperature direct electrochemical study of metalloproteins from hyperthermophilic microorganisms involves in hydrogen production from pyruvate},
author = {Smith, E T and Blamey, J and Zhou, Z Z and Adams, M W.W.},
abstractNote = {The hyperthomophilic bacterium Thermotoga maritima and the hyperthermolic archaeon Pyrococcus furiosus grow optimally at 80{degrees} and 100{degrees}C, respectively, by the fermentation of carbohydrates to organic acids, CO{sub 2}, and H{sub 2}. Pyruvate is a major source of reductant for H{sub 2} production during fermentation, and pyruvate ferredoxin oxidoreductase (POR), a 4Fe-type ferredoxin, and hydrogenase have been previously purified from both species. P. furiosus utilizes copper-iron-containing POR and a nickel-iron-containing hydrogenase, whereas the POR of T. maritima lacks copper and its hydrogenase lacks nickel. For all four enzymes and for the two ferredoxins, we have determined their reproduction potentials (E{degrees}` and, where possible, thermodynamic parameters associated with electron transfer {Delta}S{degrees} and {Delta}H{degrees}), using differential pulse voltammetry at temperatures ranging from 25 to 95{degrees}C. 55 refs., 7 fig., 2 tabs.},
doi = {10.1021/bi00021a030},
url = {https://www.osti.gov/biblio/526065},
journal = {Biochemistry (Eaton)},
number = 21,
volume = 34,
place = {United States},
year = {Tue May 30 00:00:00 EDT 1995},
month = {Tue May 30 00:00:00 EDT 1995}
}