Inhibition of hydrogen uptake in escherichia coli by expressing the hydrogenase from the Cyanobacterium Synechocystis Sp. Pcc 6803

Toshinari Maeda, Gönül Vardar, William T. Self, Thomas Keith Wood

Research output: Chapter in Book/Report/Conference proceedingConference contribution

4 Citations (Scopus)

Abstract

Molecular hydrogen is an environmentally-clean fuel and the reversible (bi-directional) hydrogenase of the cyanobacterium Synechocystis sp. PCC 6803 as well as the native Escherichia coli hydrogenase 3 hold great promise for hydrogen generation. The reversible (bi-directional) hydrogenase (hoxEFUYH) of Synechocystis sp. PCC 6803 is a [NiFe]-type enzyme that produces hydrogen via the reaction 2H+ + 2e- ↔ H2 (g); the source of the two electrons is NADH. Hydrogenase enzymes in E. coli are involved in two distinct modes of hydrogen metabolism: hydrogen production via hydrogenase 3 (encoded by hycABCDEFGHI) and hydrogen uptake by hydrogenase 1 (encoded by hyaABCDEF) and hydrogenase 2 (encoded by hybOABCDEFG). A study was conducted to determine how the cyanobacterial locus increases hydrogen production. Different components of the cyanobacterial locus were expressed. Overexpression of HoxU alone (small diaphorase subunit) accounted for 43% of the additional hydrogen produced by HoxEFUYH. Hydrogen production in TG1/pBS(Kan)HoxUYH was somewhat better than that in TG1/pBS(Kan)Synhox indicating the importance of proteins HoxU, HoxY, and HoxH. This is an abstract of a paper presented at the AIChE Annual Meeting (Salt Lake City, UT 11/4-9/2007).

Original languageEnglish (US)
Title of host publication2007 AIChE Annual Meeting
StatePublished - Dec 1 2007
Event2007 AIChE Annual Meeting - Salt Lake City, UT, United States
Duration: Nov 4 2007Nov 9 2007

Publication series

Name2007 AIChE Annual Meeting

Other

Other2007 AIChE Annual Meeting
CountryUnited States
CitySalt Lake City, UT
Period11/4/0711/9/07

Fingerprint

Synechocystis
Hydrogenase
Cyanobacteria
Escherichia coli
Hydrogen
Hydrogen production
Enzymes
Metabolism
NAD
Proteins
Electrons

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Chemical Engineering(all)
  • Bioengineering
  • Safety, Risk, Reliability and Quality

Cite this

Maeda, T., Vardar, G., Self, W. T., & Wood, T. K. (2007). Inhibition of hydrogen uptake in escherichia coli by expressing the hydrogenase from the Cyanobacterium Synechocystis Sp. Pcc 6803. In 2007 AIChE Annual Meeting (2007 AIChE Annual Meeting).
Maeda, Toshinari ; Vardar, Gönül ; Self, William T. ; Wood, Thomas Keith. / Inhibition of hydrogen uptake in escherichia coli by expressing the hydrogenase from the Cyanobacterium Synechocystis Sp. Pcc 6803. 2007 AIChE Annual Meeting. 2007. (2007 AIChE Annual Meeting).
@inproceedings{87701b57e8084e1b96c3285335249dbf,
title = "Inhibition of hydrogen uptake in escherichia coli by expressing the hydrogenase from the Cyanobacterium Synechocystis Sp. Pcc 6803",
abstract = "Molecular hydrogen is an environmentally-clean fuel and the reversible (bi-directional) hydrogenase of the cyanobacterium Synechocystis sp. PCC 6803 as well as the native Escherichia coli hydrogenase 3 hold great promise for hydrogen generation. The reversible (bi-directional) hydrogenase (hoxEFUYH) of Synechocystis sp. PCC 6803 is a [NiFe]-type enzyme that produces hydrogen via the reaction 2H+ + 2e- ↔ H2 (g); the source of the two electrons is NADH. Hydrogenase enzymes in E. coli are involved in two distinct modes of hydrogen metabolism: hydrogen production via hydrogenase 3 (encoded by hycABCDEFGHI) and hydrogen uptake by hydrogenase 1 (encoded by hyaABCDEF) and hydrogenase 2 (encoded by hybOABCDEFG). A study was conducted to determine how the cyanobacterial locus increases hydrogen production. Different components of the cyanobacterial locus were expressed. Overexpression of HoxU alone (small diaphorase subunit) accounted for 43{\%} of the additional hydrogen produced by HoxEFUYH. Hydrogen production in TG1/pBS(Kan)HoxUYH was somewhat better than that in TG1/pBS(Kan)Synhox indicating the importance of proteins HoxU, HoxY, and HoxH. This is an abstract of a paper presented at the AIChE Annual Meeting (Salt Lake City, UT 11/4-9/2007).",
author = "Toshinari Maeda and G{\"o}n{\"u}l Vardar and Self, {William T.} and Wood, {Thomas Keith}",
year = "2007",
month = "12",
day = "1",
language = "English (US)",
isbn = "9780816910229",
series = "2007 AIChE Annual Meeting",
booktitle = "2007 AIChE Annual Meeting",

}

Maeda, T, Vardar, G, Self, WT & Wood, TK 2007, Inhibition of hydrogen uptake in escherichia coli by expressing the hydrogenase from the Cyanobacterium Synechocystis Sp. Pcc 6803. in 2007 AIChE Annual Meeting. 2007 AIChE Annual Meeting, 2007 AIChE Annual Meeting, Salt Lake City, UT, United States, 11/4/07.

Inhibition of hydrogen uptake in escherichia coli by expressing the hydrogenase from the Cyanobacterium Synechocystis Sp. Pcc 6803. / Maeda, Toshinari; Vardar, Gönül; Self, William T.; Wood, Thomas Keith.

2007 AIChE Annual Meeting. 2007. (2007 AIChE Annual Meeting).

Research output: Chapter in Book/Report/Conference proceedingConference contribution

TY - GEN

T1 - Inhibition of hydrogen uptake in escherichia coli by expressing the hydrogenase from the Cyanobacterium Synechocystis Sp. Pcc 6803

AU - Maeda, Toshinari

AU - Vardar, Gönül

AU - Self, William T.

AU - Wood, Thomas Keith

PY - 2007/12/1

Y1 - 2007/12/1

N2 - Molecular hydrogen is an environmentally-clean fuel and the reversible (bi-directional) hydrogenase of the cyanobacterium Synechocystis sp. PCC 6803 as well as the native Escherichia coli hydrogenase 3 hold great promise for hydrogen generation. The reversible (bi-directional) hydrogenase (hoxEFUYH) of Synechocystis sp. PCC 6803 is a [NiFe]-type enzyme that produces hydrogen via the reaction 2H+ + 2e- ↔ H2 (g); the source of the two electrons is NADH. Hydrogenase enzymes in E. coli are involved in two distinct modes of hydrogen metabolism: hydrogen production via hydrogenase 3 (encoded by hycABCDEFGHI) and hydrogen uptake by hydrogenase 1 (encoded by hyaABCDEF) and hydrogenase 2 (encoded by hybOABCDEFG). A study was conducted to determine how the cyanobacterial locus increases hydrogen production. Different components of the cyanobacterial locus were expressed. Overexpression of HoxU alone (small diaphorase subunit) accounted for 43% of the additional hydrogen produced by HoxEFUYH. Hydrogen production in TG1/pBS(Kan)HoxUYH was somewhat better than that in TG1/pBS(Kan)Synhox indicating the importance of proteins HoxU, HoxY, and HoxH. This is an abstract of a paper presented at the AIChE Annual Meeting (Salt Lake City, UT 11/4-9/2007).

AB - Molecular hydrogen is an environmentally-clean fuel and the reversible (bi-directional) hydrogenase of the cyanobacterium Synechocystis sp. PCC 6803 as well as the native Escherichia coli hydrogenase 3 hold great promise for hydrogen generation. The reversible (bi-directional) hydrogenase (hoxEFUYH) of Synechocystis sp. PCC 6803 is a [NiFe]-type enzyme that produces hydrogen via the reaction 2H+ + 2e- ↔ H2 (g); the source of the two electrons is NADH. Hydrogenase enzymes in E. coli are involved in two distinct modes of hydrogen metabolism: hydrogen production via hydrogenase 3 (encoded by hycABCDEFGHI) and hydrogen uptake by hydrogenase 1 (encoded by hyaABCDEF) and hydrogenase 2 (encoded by hybOABCDEFG). A study was conducted to determine how the cyanobacterial locus increases hydrogen production. Different components of the cyanobacterial locus were expressed. Overexpression of HoxU alone (small diaphorase subunit) accounted for 43% of the additional hydrogen produced by HoxEFUYH. Hydrogen production in TG1/pBS(Kan)HoxUYH was somewhat better than that in TG1/pBS(Kan)Synhox indicating the importance of proteins HoxU, HoxY, and HoxH. This is an abstract of a paper presented at the AIChE Annual Meeting (Salt Lake City, UT 11/4-9/2007).

UR - http://www.scopus.com/inward/record.url?scp=58049119496&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=58049119496&partnerID=8YFLogxK

M3 - Conference contribution

AN - SCOPUS:58049119496

SN - 9780816910229

T3 - 2007 AIChE Annual Meeting

BT - 2007 AIChE Annual Meeting

ER -

Maeda T, Vardar G, Self WT, Wood TK. Inhibition of hydrogen uptake in escherichia coli by expressing the hydrogenase from the Cyanobacterium Synechocystis Sp. Pcc 6803. In 2007 AIChE Annual Meeting. 2007. (2007 AIChE Annual Meeting).