Microsoft word - fakultaetsbroschuere_stand10122003.doc
Walter G. Zumft
Nitrate and nitric oxide, in addition to being respiratory substrates, are signal molecules for the induction of N-oxide-metabolizing enzymes. The NO signal is processed by transcription factors of the Crp-Fnr superfamily. Denitrification is intimately related to other cellular processes such as primary and secondary transport, protein translocation, cytochrome c
biogenesis, anaerobic and N-oxide-dependent gene regulation, metalloprotein assembly, and the biosynthesis of cofactors. Thus, the research topic provides a
fascinating area for interdisciplinary approaches
Full Professor. Microbiology since 1982. Biology
diploma 1968, Doctoral degree 1970, Habilitation
1974, Assoc. Professor 1980, University of
Erlangen-Nürnberg. 1971-74 Research Associate,
Purdue University, West Lafayette, IN. 1978-79
Visiting Professor, University of Georgia, Athens,
GA, 1980 Visiting Scientist, Arrhenius Laboratory,
University of Stockholm.
Phone: +49-721-608-3473; Fax: -8932; e-mail:
Principal Research Interests
Denitrification provides a distinct mode of bacterial
energy conservation. It makes use of N-oxides as
terminal electron acceptors for cellular
bioenergetics and thereby reverses dinitrogen
fixation. The process is part of the global N-cycle,
Körner, H., Sofia, H., Zumft, W. G. (2003) Phylogeny of
essential for all life forms. Our main research
the bacterial superfamily of Crp-Fnr transcription regulators: exploiting the metabolic spectrum by
controlling alternative gene programs. FEMS Microbiol.
Wunsch, P., Herb, M., Wieland, H., Schiek, U., and Zumft, W. G. (2003) Requirements for CuA and Cu-S center assembly of nitrous oxide reductase deduced from complete periplasmic enzyme maturation in the nondenitrifier Pseudomonas putida
. J. Bacteriol., 185:887-896.
3. Zumft, W. G. (2002) Nitric oxide signaling and NO
dependent transcriptional control in bacterial denitrification by members of the Fnr-Crp regulator family. J. Mol. Microbiol. Biotechnol., 4:277-286.
Alvarez, M. L., Ai, J., Zumft, W. G., Sanders-Loehr, J.,
Dooley, D. M. (2001) Characterization of the copper-sulfur
chromophores in nitrous oxide reductase by resonance
The activation and enzymatic transformation of N-
Raman spectroscopy: evidence for sulfur coordination in the catalytic cluster. J. Am. Chem. Soc., 123:576-587.
oxides is based on Fe, Cu, and Mo and their redox
Charnock, J., Dreusch, A. Körner, H., Neese, F., Nelson, J.,
chemistry. The metal ions are found in the
Kannt, A., Michel, H., Garner, D., Kroneck, P. M. H.,
denitrification enzymes in distinct organic cofactors
Zumft, W. G. (2000) Structural investigations of the CuA
or as protein-bound metal clusters. We have
center of nitrous oxide reductase from Pseudomonas stutzeri
by site-directed mutagenesis and X-ray absorption
isolated the novel enzymes nitric oxide reductase
spectroscopy. Eur. J. Biochem., 267:1368-1381.
and nitrous oxide reductase, and provided their first
Härtig, E., Schiek, U., Vollack, K-U., Zumft, W. G. (1999)
biochemical characterization and access to the
Nitrate and nitrite control of respiratory nitrate reduction in
genetic basis of the process. Around 40 genes are
denitrifying Pseudomonas stutzeri
by a two-component regulatory system homologous to NarXL of Escherichia
required to encode the core structures of the
. J. Bacteriol., 181:3658-3665.
Zumft, W. G. (1997) Cell biology and molecular basis of
We are investigating the components of the
denitrification. Microbiol. Mol. Biol. Rev., 61:533-616.
process, their topology with respect to the bacterial cytoplasmic membrane, and their regulation.
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