TY - GEN
T1 - Proteomic analysis of a hydrogen producing thermophile carboxydothermus hydrogenoformans
AU - Thompson, Vicki S.
AU - Epting, Kevin
AU - Schaller, Kastli D.
AU - Reed, David W.
PY - 2006
Y1 - 2006
N2 - The development of an economic means of hydrogen production is necessary before H2 can be widely implemented as a replacement for fossil fuels. Currently, the majority of H2 produced in the US is generated through steam reforming of natural gas or coal gasification, both energy intensive processes. To fully utilize and optimize microbial H2 production, it is necessary to understand how the CO metabolic process functions. A thermophilic carboxydotroph, Carboxydothermus hydrogenoformans, was selected as a model organism for studies of CO metabolism employing proteomic methodologies. Protein expression was compared under different growth conditions: 0.05 g/L vs. 0.5 g/L yeast extract, and AQDS CO free vs. pure CO headspace. Analysis of the MS/MS data from the soluble fraction identified peptides corresponding to over 15 different proteins from C. hydrogenoformans. Two of the proteins identified were the cooS II (CHY_0085) and cooS IV (CHY_1824) CODH subunits. Four peptides from CHY_0085 and three from CHY_1824 were identified with significant probability. This is an abstract of a paper presented at the AIChE Annual Meeting (San Francisco, CA 11/12-17/2006).
AB - The development of an economic means of hydrogen production is necessary before H2 can be widely implemented as a replacement for fossil fuels. Currently, the majority of H2 produced in the US is generated through steam reforming of natural gas or coal gasification, both energy intensive processes. To fully utilize and optimize microbial H2 production, it is necessary to understand how the CO metabolic process functions. A thermophilic carboxydotroph, Carboxydothermus hydrogenoformans, was selected as a model organism for studies of CO metabolism employing proteomic methodologies. Protein expression was compared under different growth conditions: 0.05 g/L vs. 0.5 g/L yeast extract, and AQDS CO free vs. pure CO headspace. Analysis of the MS/MS data from the soluble fraction identified peptides corresponding to over 15 different proteins from C. hydrogenoformans. Two of the proteins identified were the cooS II (CHY_0085) and cooS IV (CHY_1824) CODH subunits. Four peptides from CHY_0085 and three from CHY_1824 were identified with significant probability. This is an abstract of a paper presented at the AIChE Annual Meeting (San Francisco, CA 11/12-17/2006).
UR - https://www.scopus.com/pages/publications/58049098458
M3 - Conference contribution
AN - SCOPUS:58049098458
SN - 081691012X
SN - 9780816910120
T3 - AIChE Annual Meeting, Conference Proceedings
BT - 2006 AIChE Annual Meeting
T2 - 2006 AIChE Annual Meeting
Y2 - 12 November 2006 through 17 November 2006
ER -