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Involvement of hydrogenases in the formation of highly catalytic Pd(0) nanoparticles by bioreduction of Pd(II) using Escherichia coli mutant strains

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Involvement of hydrogenases in the formation of highly catalytic Pd(0) nanoparticles by bioreduction of Pd(II) using Escherichia coli mutant strains. / Deplanche, Kevin; Caldelari, Isabelle; Mikheenko, Iryna P.; Sargent, Frank; Macaskie, Lynne E.

In: Microbiology-SGM, Vol. 156, No. 9, 09.2010, p. 2630-2640.

Research output: Contribution to journalArticle

Harvard

Deplanche, K, Caldelari, I, Mikheenko, IP, Sargent, F & Macaskie, LE 2010, 'Involvement of hydrogenases in the formation of highly catalytic Pd(0) nanoparticles by bioreduction of Pd(II) using Escherichia coli mutant strains' Microbiology-SGM, vol 156, no. 9, pp. 2630-2640., 10.1099/mic.0.036681-0

APA

Deplanche, K., Caldelari, I., Mikheenko, I. P., Sargent, F., & Macaskie, L. E. (2010). Involvement of hydrogenases in the formation of highly catalytic Pd(0) nanoparticles by bioreduction of Pd(II) using Escherichia coli mutant strains. Microbiology-SGM, 156(9), 2630-2640. 10.1099/mic.0.036681-0

Vancouver

Deplanche K, Caldelari I, Mikheenko IP, Sargent F, Macaskie LE. Involvement of hydrogenases in the formation of highly catalytic Pd(0) nanoparticles by bioreduction of Pd(II) using Escherichia coli mutant strains. Microbiology-SGM. 2010 Sep;156(9):2630-2640. Available from: 10.1099/mic.0.036681-0

Author

Deplanche, Kevin; Caldelari, Isabelle; Mikheenko, Iryna P.; Sargent, Frank; Macaskie, Lynne E. / Involvement of hydrogenases in the formation of highly catalytic Pd(0) nanoparticles by bioreduction of Pd(II) using Escherichia coli mutant strains.

In: Microbiology-SGM, Vol. 156, No. 9, 09.2010, p. 2630-2640.

Research output: Contribution to journalArticle

Bibtex - Download

@article{d869440cd039464ca51c8f4f049374ff,
title = "Involvement of hydrogenases in the formation of highly catalytic Pd(0) nanoparticles by bioreduction of Pd(II) using Escherichia coli mutant strains",
keywords = "SULFATE-REDUCING BACTERIA, DESULFOVIBRIO-DESULFURICANS, POLYCHLORINATED-BIPHENYLS, BIOINORGANIC CATALYST, MICROBIAL REDUCTION, METAL REDUCTION, PALLADIUM, GOLD, RECOVERY, REMOVAL",
author = "Kevin Deplanche and Isabelle Caldelari and Mikheenko, {Iryna P.} and Frank Sargent and Macaskie, {Lynne E.}",
year = "2010",
doi = "10.1099/mic.0.036681-0",
volume = "156",
number = "9",
pages = "2630--2640",
journal = "Microbiology-SGM",
issn = "1350-0872",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - Involvement of hydrogenases in the formation of highly catalytic Pd(0) nanoparticles by bioreduction of Pd(II) using Escherichia coli mutant strains

A1 - Deplanche,Kevin

A1 - Caldelari,Isabelle

A1 - Mikheenko,Iryna P.

A1 - Sargent,Frank

A1 - Macaskie,Lynne E.

AU - Deplanche,Kevin

AU - Caldelari,Isabelle

AU - Mikheenko,Iryna P.

AU - Sargent,Frank

AU - Macaskie,Lynne E.

PY - 2010/9

Y1 - 2010/9

N2 - <p>Escherichia coil produces at least three [NiFe] hydrogenases (Hyd-1, Hyd-2 and Hyd-3). Hyd-1 and Hyd-2 are membrane-bound respiratory isoenzymes with their catalytic subunits exposed to the periplasmic side of the membrane. Hyd-3 is part of the cytoplasmically oriented formate hydrogenlyase complex. In this work the involvement of each of these hydrogenases in Pd(II) reduction under acidic (pH 2.4) conditions was studied. While all three hydrogenases could contribute to Pd(II) reduction, the presence of either periplasmic hydrogenase (Hyd-1 or Hyd-2) was required to observe Pd(II) reduction rates comparable to the parent strain. An E. coli mutant strain genetically deprived of all hydrogenase activity showed negligible Pd(II) reduction. Electron microscopy suggested that the location of the resulting Pd(0) deposits was as expected from the subcellular localization of the particular hydrogenase involved in the reduction process. Membrane separation experiments established that Pd(II) reductase activity is membrane-bound and that hydrogenases are required to initiate Pd(II) reduction. The catalytic activity of the resulting Pd(0) nanoparticles in the reduction of Cr(VI) to Cr(III) varied according to the E. coli mutant strain used for the initial bioreduction of Pd(II). Optimum Cr(VI) reduction, comparable to that observed with a commercial Pd catalyst, was observed when the bio-Pd(0) catalytic particles were prepared from a strain containing an active Hyd-1. The results are discussed in the context of economic production of novel nanometallic catalysts.</p>

AB - <p>Escherichia coil produces at least three [NiFe] hydrogenases (Hyd-1, Hyd-2 and Hyd-3). Hyd-1 and Hyd-2 are membrane-bound respiratory isoenzymes with their catalytic subunits exposed to the periplasmic side of the membrane. Hyd-3 is part of the cytoplasmically oriented formate hydrogenlyase complex. In this work the involvement of each of these hydrogenases in Pd(II) reduction under acidic (pH 2.4) conditions was studied. While all three hydrogenases could contribute to Pd(II) reduction, the presence of either periplasmic hydrogenase (Hyd-1 or Hyd-2) was required to observe Pd(II) reduction rates comparable to the parent strain. An E. coli mutant strain genetically deprived of all hydrogenase activity showed negligible Pd(II) reduction. Electron microscopy suggested that the location of the resulting Pd(0) deposits was as expected from the subcellular localization of the particular hydrogenase involved in the reduction process. Membrane separation experiments established that Pd(II) reductase activity is membrane-bound and that hydrogenases are required to initiate Pd(II) reduction. The catalytic activity of the resulting Pd(0) nanoparticles in the reduction of Cr(VI) to Cr(III) varied according to the E. coli mutant strain used for the initial bioreduction of Pd(II). Optimum Cr(VI) reduction, comparable to that observed with a commercial Pd catalyst, was observed when the bio-Pd(0) catalytic particles were prepared from a strain containing an active Hyd-1. The results are discussed in the context of economic production of novel nanometallic catalysts.</p>

KW - SULFATE-REDUCING BACTERIA

KW - DESULFOVIBRIO-DESULFURICANS

KW - POLYCHLORINATED-BIPHENYLS

KW - BIOINORGANIC CATALYST

KW - MICROBIAL REDUCTION

KW - METAL REDUCTION

KW - PALLADIUM

KW - GOLD

KW - RECOVERY

KW - REMOVAL

U2 - 10.1099/mic.0.036681-0

DO - 10.1099/mic.0.036681-0

M1 - Article

JO - Microbiology-SGM

JF - Microbiology-SGM

SN - 1350-0872

IS - 9

VL - 156

SP - 2630

EP - 2640

ER -

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