Literature DB >> 20979125

Interaction of CO dehydrogenase with the cytoplasmic membrane monitored by fluorescence correlation spectroscopy.

Florian Spreitler1, Christian Brock, Astrid Pelzmann, Ortwin Meyer, Jürgen Köhler.   

Abstract

We have investigated the interaction of carbon monoxide dehydrogenase (CODH), an enzyme that catalyses the oxidation of CO in the aerobic eubacterium Oligotropha carboxidovorans, with the cytoplasmic membrane by using fluorescence correlation spectroscopy (FCS). Our results reveal that in vitro this interaction of CODH is specific for cytoplasmic membranes from CO-grown bacteria.

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Year:  2010        PMID： 20979125     DOI： 10.1002/cbic.201000431

Source DB:  PubMed          Journal:  Chembiochem        ISSN： 1439-4227            Impact factor:   3.164


  3 in total

Review 1.  The aerobic CO dehydrogenase from Oligotropha carboxidovorans.

Authors:  Russ Hille; Stephanie Dingwall; Jarett Wilcoxen
Journal:  J Biol Inorg Chem       Date:  2014-08-26       Impact factor: 3.358

Review 2.  The mononuclear molybdenum enzymes.

Authors:  Russ Hille; James Hall; Partha Basu
Journal:  Chem Rev       Date:  2014-01-28       Impact factor: 60.622

3.  3-Hydroxypyridine Dehydrogenase HpdA Is Encoded by a Novel Four-Component Gene Cluster and Catalyzes the First Step of 3-Hydroxypyridine Catabolism in Ensifer adhaerens HP1.

Authors:  Haixia Wang; Xiaoyu Wang; Hao Ren; Xuejun Wang; Zhenmei Lu
Journal:  Appl Environ Microbiol       Date:  2020-09-17       Impact factor: 4.792
  3 in total

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