The archetype γ-class carbonic anhydrase (cam) contains iron when synthesized in vivo

Sheridan R. MacAuley; Sabrina A. Zimmerman; Ethel E. Apolinario; Caryn Evilia; Ya Ming Hou; James G. Ferry; Kevin R. Sowers

doi:10.1021/bi802246s

The archetype γ-class carbonic anhydrase (cam) contains iron when synthesized in vivo

Sheridan R. MacAuley, Sabrina A. Zimmerman, Ethel E. Apolinario, Caryn Evilia, Ya Ming Hou, James G. Ferry, Kevin R. Sowers

Biochemistry & Molecular Biology

Research output: Contribution to journal › Article › peer-review

81 Scopus citations

Abstract

A recombinant protein overproduction system was developed in Methanosarcina acetiVorans to facilitate biochemical characterization of oxygen-sensitive metal-loenzymes from strictly anaerobic species in the Archaea domain. The system was used to overproduce the archetype of the independently evolved γ-class carbonic anhydrase. The overproduced enzyme was oxygen sensitive and had full incorporation of iron instead of zinc observed when overproduced in Escherichia coli. This, the first report of in vivo iron incorporation for any carbonic anhydrase, supports the need to reevaluate the role of iron in all classes of carbonic anhydrases derived from anaerobic environments.

Original language	English (US)
Pages (from-to)	817-819
Number of pages	3
Journal	Biochemistry
Volume	48
Issue number	5
DOIs	https://doi.org/10.1021/bi802246s
State	Published - Feb 10 2009

All Science Journal Classification (ASJC) codes

Biochemistry

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10.1021/bi802246s

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title = "The archetype γ-class carbonic anhydrase (cam) contains iron when synthesized in vivo",

abstract = "A recombinant protein overproduction system was developed in Methanosarcina acetiVorans to facilitate biochemical characterization of oxygen-sensitive metal-loenzymes from strictly anaerobic species in the Archaea domain. The system was used to overproduce the archetype of the independently evolved γ-class carbonic anhydrase. The overproduced enzyme was oxygen sensitive and had full incorporation of iron instead of zinc observed when overproduced in Escherichia coli. This, the first report of in vivo iron incorporation for any carbonic anhydrase, supports the need to reevaluate the role of iron in all classes of carbonic anhydrases derived from anaerobic environments.",

author = "MacAuley, {Sheridan R.} and Zimmerman, {Sabrina A.} and Apolinario, {Ethel E.} and Caryn Evilia and Hou, {Ya Ming} and Ferry, {James G.} and Sowers, {Kevin R.}",

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AU - MacAuley, Sheridan R.

AU - Zimmerman, Sabrina A.

AU - Apolinario, Ethel E.

AU - Evilia, Caryn

AU - Hou, Ya Ming

AU - Ferry, James G.

AU - Sowers, Kevin R.

PY - 2009/2/10

Y1 - 2009/2/10

N2 - A recombinant protein overproduction system was developed in Methanosarcina acetiVorans to facilitate biochemical characterization of oxygen-sensitive metal-loenzymes from strictly anaerobic species in the Archaea domain. The system was used to overproduce the archetype of the independently evolved γ-class carbonic anhydrase. The overproduced enzyme was oxygen sensitive and had full incorporation of iron instead of zinc observed when overproduced in Escherichia coli. This, the first report of in vivo iron incorporation for any carbonic anhydrase, supports the need to reevaluate the role of iron in all classes of carbonic anhydrases derived from anaerobic environments.

AB - A recombinant protein overproduction system was developed in Methanosarcina acetiVorans to facilitate biochemical characterization of oxygen-sensitive metal-loenzymes from strictly anaerobic species in the Archaea domain. The system was used to overproduce the archetype of the independently evolved γ-class carbonic anhydrase. The overproduced enzyme was oxygen sensitive and had full incorporation of iron instead of zinc observed when overproduced in Escherichia coli. This, the first report of in vivo iron incorporation for any carbonic anhydrase, supports the need to reevaluate the role of iron in all classes of carbonic anhydrases derived from anaerobic environments.

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The archetype γ-class carbonic anhydrase (cam) contains iron when synthesized in vivo

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