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Journal of Bacteriology, July 2005, p. 4505-4513, Vol. 187, No. 13
0021-9193/05/$08.00+0     doi:10.1128/JB.187.13.4505-4513.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

OmcF, a Putative c-Type Monoheme Outer Membrane Cytochrome Required for the Expression of Other Outer Membrane Cytochromes in Geobacter sulfurreducens

Byoung-Chan Kim,* Ching Leang, Yan-Huai R. Ding, Richard H. Glaven, Maddalena V. Coppi, and Derek R. Lovley

Department of Microbiology, University of Massachusetts, Amherst, Massachusetts 01003

Received 23 November 2004/ Accepted 21 March 2005

Outer membrane cytochromes are often proposed as likely agents for electron transfer to extracellular electron acceptors, such as Fe(III). The omcF gene in the dissimilatory Fe(III)-reducing microorganism Geobacter sulfurreducens is predicted to code for a small outer membrane monoheme c-type cytochrome. An OmcF-deficient strain was constructed, and its ability to reduce and grow on Fe(III) citrate was found to be impaired. Following a prolonged lag phase (150 h), the OmcF-deficient strain developed the ability to grow in Fe(III) citrate medium with doubling times and yields that were ca. 145% and 70% of those of the wild type, respectively. Comparison of the c-type cytochrome contents of outer membrane-enriched fractions prepared from wild-type and OmcF-deficient cultures confirmed the outer membrane association of OmcF and revealed multiple changes in the cytochrome content of the OmcF-deficient strain. These changes included loss of expression of two previously characterized outer membrane cytochromes, OmcB and OmcC, and overexpression of a third previously characterized outer membrane cytochrome, OmcS, during growth on Fe(III) citrate. The omcB and omcC transcripts could not be detected in the OmcF-deficient mutant by either reverse transcriptase PCR or Northern blot analyses. Expression of the omcF gene in trans restored both the capacity of the OmcF-deficient mutant to reduce Fe(III) and wild-type levels of omcB and omcC mRNA and protein. Thus, elimination of OmcF may impair Fe(III) reduction by influencing expression of OmcB, which has previously been demonstrated to play a critical role in Fe(III) reduction.

* Corresponding author. Mailing address: Department of Microbiology, 203 Morrill Science IVN, University of Massachusetts at Amherst, 639 North Pleasant St., Amherst, MA 01003. Phone: (413) 545-6796. Fax: (413) 545-1578. E-mail: bckim{at}microbio.umass.edu.

Journal of Bacteriology, July 2005, p. 4505-4513, Vol. 187, No. 13
0021-9193/05/$08.00+0     doi:10.1128/JB.187.13.4505-4513.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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