DETECTION OF THE IN-VIVO INCORPORATION OF A METAL CLUSTER INTO A PROTEIN - THE FEMO COFACTOR IS INSERTED INTO THE FEFE PROTEIN OF THE ALTERNATIVE NITROGENASE OF RHODOBACTER-CAPSULATUS

GOLLAN U, Schneider K, Müller A, SCHUDDEKOPF K, KLIPP W (1993)
EUROPEAN JOURNAL OF BIOCHEMISTRY 215(1): 25-35.

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Abstract
The photosynthetic bacterium Rhodobacter capsulatus has, in addition to the Mo nitrogenase, a second Mo-independent nitrogen-fixing system, an 'iron-only' nitrogenase which is strongly repressed by molybdate. The MoO42- concentration causing 50% repression of the alternative nitrogenase in nifHDK- cells was 6 nM. If MoO42- was added to a growing nifHDK- culture which had already expressed the alternative nitrogenase, the production of ethane from acetylene, by whole cells, was stimulated dramatically. In spite of the fact that C2H4 formation decreased continuously during the duration of the experiment (3 days), the total C2H6 Production increased about twofold within the first 24 h, whereas the relative yield of C2H6 increased from 2% (C2H6/C2H4 X 100) in the absence of MoO42-, to a maximal value of 69% in the presence of MoO42- (1 mM) after 72 h incubation. This 'Mo effect' appeared to be stronger the higher the MoO42- concentration in the medium and the longer the incubation time. In the presence of ReO4-, WO42- or VO43-, a similar effect did not occur. The 'Mo effect' was not observed in a nifHDK-nifE- double mutant which is unable to synthesize the FeMo cofactor and was diminished in a nifHDK-nifQ- mutant. Crude extracts from nifHDK- cells cultivated in the presence of MoO42-, also showed enhanced production of ethane. Component 1, purified from those extracts, displayed an S = 3/2 EPR signal which was relatively weak but characteristic for the FeMoco. These results strongly support the suggestion that the 'Mo effect' is a consequence of the formation of a hybrid enzyme consisting of the apoprotein of the alternative nitrogenase and the FeMo cofactor of the conventional nitrogenase. The 'Mo effect' was not influenced by the addition of chloramphenicol to the cultures. The occurrence of the 'Mo effect' appeared, therefore, to be independent of de-novo protein synthesis. The analysis of nifE-lacZ and nifN-lacZ fusions proved that both genes necessary for the FeMo cofactor synthesis are also expressed under conditions of MoO42- deficiency. The possible explanations for incorporation of the FeMoco into component 1 of the alternative nitrogenase are discussed.
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GOLLAN U, Schneider K, Müller A, SCHUDDEKOPF K, KLIPP W. DETECTION OF THE IN-VIVO INCORPORATION OF A METAL CLUSTER INTO A PROTEIN - THE FEMO COFACTOR IS INSERTED INTO THE FEFE PROTEIN OF THE ALTERNATIVE NITROGENASE OF RHODOBACTER-CAPSULATUS. EUROPEAN JOURNAL OF BIOCHEMISTRY. 1993;215(1):25-35.
GOLLAN, U., Schneider, K., Müller, A., SCHUDDEKOPF, K., & KLIPP, W. (1993). DETECTION OF THE IN-VIVO INCORPORATION OF A METAL CLUSTER INTO A PROTEIN - THE FEMO COFACTOR IS INSERTED INTO THE FEFE PROTEIN OF THE ALTERNATIVE NITROGENASE OF RHODOBACTER-CAPSULATUS. EUROPEAN JOURNAL OF BIOCHEMISTRY, 215(1), 25-35.
GOLLAN, U., Schneider, K., Müller, A., SCHUDDEKOPF, K., and KLIPP, W. (1993). DETECTION OF THE IN-VIVO INCORPORATION OF A METAL CLUSTER INTO A PROTEIN - THE FEMO COFACTOR IS INSERTED INTO THE FEFE PROTEIN OF THE ALTERNATIVE NITROGENASE OF RHODOBACTER-CAPSULATUS. EUROPEAN JOURNAL OF BIOCHEMISTRY 215, 25-35.
GOLLAN, U., et al., 1993. DETECTION OF THE IN-VIVO INCORPORATION OF A METAL CLUSTER INTO A PROTEIN - THE FEMO COFACTOR IS INSERTED INTO THE FEFE PROTEIN OF THE ALTERNATIVE NITROGENASE OF RHODOBACTER-CAPSULATUS. EUROPEAN JOURNAL OF BIOCHEMISTRY, 215(1), p 25-35.
U. GOLLAN, et al., “DETECTION OF THE IN-VIVO INCORPORATION OF A METAL CLUSTER INTO A PROTEIN - THE FEMO COFACTOR IS INSERTED INTO THE FEFE PROTEIN OF THE ALTERNATIVE NITROGENASE OF RHODOBACTER-CAPSULATUS”, EUROPEAN JOURNAL OF BIOCHEMISTRY, vol. 215, 1993, pp. 25-35.
GOLLAN, U., Schneider, K., Müller, A., SCHUDDEKOPF, K., KLIPP, W.: DETECTION OF THE IN-VIVO INCORPORATION OF A METAL CLUSTER INTO A PROTEIN - THE FEMO COFACTOR IS INSERTED INTO THE FEFE PROTEIN OF THE ALTERNATIVE NITROGENASE OF RHODOBACTER-CAPSULATUS. EUROPEAN JOURNAL OF BIOCHEMISTRY. 215, 25-35 (1993).
GOLLAN, U, Schneider, Klaus, Müller, Achim, SCHUDDEKOPF, K, and KLIPP, W. “DETECTION OF THE IN-VIVO INCORPORATION OF A METAL CLUSTER INTO A PROTEIN - THE FEMO COFACTOR IS INSERTED INTO THE FEFE PROTEIN OF THE ALTERNATIVE NITROGENASE OF RHODOBACTER-CAPSULATUS”. EUROPEAN JOURNAL OF BIOCHEMISTRY 215.1 (1993): 25-35.
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12 Citations in Europe PMC

Data provided by Europe PubMed Central.

Reconstruction and minimal gene requirements for the alternative iron-only nitrogenase in Escherichia coli.
Yang J, Xie X, Wang X, Dixon R, Wang YP., Proc. Natl. Acad. Sci. U.S.A. 111(35), 2014
PMID: 25139995
Coordinated expression of fdxD and molybdenum nitrogenase genes promotes nitrogen fixation by Rhodobacter capsulatus in the presence of oxygen.
Hoffmann MC, Muller A, Fehringer M, Pfander Y, Narberhaus F, Masepohl B., J. Bacteriol. 196(3), 2014
PMID: 24272776
Effects of Mo(VI) on phototrophic hydrogen production by Rhodobacter sphaeroides.
Fang HH, Li RY, Zhang T., Environ Technol 32(11-12), 2011
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Coevolution of metal availability and nitrogen assimilation in cyanobacteria and algae.
Glass JB, Wolfe-Simon F, Anbar AD., Geobiology 7(2), 2009
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FeMo cofactor biosynthesis in a nifE- mutant of Rhodobacter capsulatus.
Siemann S, Schneider K, Behrens K, Knochel A, Klipp W, Muller A., Eur. J. Biochem. 268(7), 2001
PMID: 11277916
Comparative biochemical characterization of the iron-only nitrogenase and the molybdenum nitrogenase from Rhodobacter capsulatus.
Schneider K, Gollan U, Drottboom M, Selsemeier-Voigt S, Muller A., Eur. J. Biochem. 244(3), 1997
PMID: 9108249
Purification and characterization of the alternative nitrogenase from the photosynthetic bacterium Rhodospirillum rubrum.
Davis R, Lehman L, Petrovich R, Shah VK, Roberts GP, Ludden PW., J. Bacteriol. 178(5), 1996
PMID: 8631723
Phenotypic characterization of a tungsten-tolerant mutant of Azotobacter vinelandii.
Premakumar R, Jacobitz S, Ricke SC, Bishop PE., J. Bacteriol. 178(3), 1996
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The molybdenum nitrogenase from wild-type Xanthobacter autotrophicus exhibits properties reminiscent of alternative nitrogenases.
Schneider K, Muller A, Krahn E, Hagen WR, Wassink H, Knuttel KH., Eur. J. Biochem. 230(2), 1995
PMID: 7607241
Biosynthesis of the iron-molybdenum cofactor of nitrogenase.
Allen RM, Chatterjee R, Madden MS, Ludden PW, Shah VK., Crit. Rev. Biotechnol. 14(3), 1994
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