A new type of metalloprotein: The mo storage protein from Azotobacter vinelandii contains a polynuclear molybdenum-oxide cluster

Fenske D, Gnida M, Schneider K, Meyer-Klaucke W, Schemberg J, Henschel V, Meyer AK, Knochel A, Müller A (2005)
CHEMBIOCHEM 6(2): 405-413.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
 
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Autor*in
Fenske, Dieter; Gnida, M.; Schneider, KlausUniBi; Meyer-Klaucke, W.; Schemberg, Joerg; Henschel, V.; Meyer, A. K.; Knochel, A.; Müller, AchimUniBi
Abstract / Bemerkung
Azotobacter vinelandii is a diazotrophic bacterium characterized by the outstanding capability of storing Mo in a special storage protein, which guarantees Mo-dependent nitrogen fixation even,under growth conditions of extreme Mo starvation. The Mo storage protein is constitutively synthesized with respect to the nitrogen source and is regulated by molybdenum at an extremely low concentration level (0-50 nm). This protein was isolated as an alpha(4)beta(4) octamer with a total molecular mass of about 240 kg mol(-1) and its shape was determined by small-angle X-ray scattering. The genes of the alpha and beta subunits were unequivocally identified; the amino acid sequences thereby determined reveal that the Mo storage protein is not related to any other known molybdoprotein. Each protein molecule can store at least 90 Mo atoms. Extended X-ray absorption fine-structure spectroscopy identified a metal-oxygen cluster bound to the Mo storage protein. The binding of Mo (biosynthesis and incorporation of the duster) is de pendent on adenosine triphosphate (ATP); Mo release is ATP-independent but pH-regulated, occurring only above pH 7.1. This Mo storage protein is the only known noniron metal storage system in the biosphere containing a metal-oxygen cluster.
Stichworte
molybdenum; metal storage protein; bioinorganic chemistry; polyoxomolybdate; metalloproteins
Erscheinungsjahr
2005
Zeitschriftentitel
CHEMBIOCHEM
Band
6
Ausgabe
2
Seite(n)
405-413
ISSN
1439-4227
Page URI
https://pub.uni-bielefeld.de/record/1604979

Zitieren

Fenske D, Gnida M, Schneider K, et al. A new type of metalloprotein: The mo storage protein from Azotobacter vinelandii contains a polynuclear molybdenum-oxide cluster. CHEMBIOCHEM. 2005;6(2):405-413.
Fenske, D., Gnida, M., Schneider, K., Meyer-Klaucke, W., Schemberg, J., Henschel, V., Meyer, A. K., et al. (2005). A new type of metalloprotein: The mo storage protein from Azotobacter vinelandii contains a polynuclear molybdenum-oxide cluster. CHEMBIOCHEM, 6(2), 405-413. https://doi.org/10.1002/cbic.200400263
Fenske, Dieter, Gnida, M., Schneider, Klaus, Meyer-Klaucke, W., Schemberg, Joerg, Henschel, V., Meyer, A. K., Knochel, A., and Müller, Achim. 2005. “A new type of metalloprotein: The mo storage protein from Azotobacter vinelandii contains a polynuclear molybdenum-oxide cluster”. CHEMBIOCHEM 6 (2): 405-413.
Fenske, D., Gnida, M., Schneider, K., Meyer-Klaucke, W., Schemberg, J., Henschel, V., Meyer, A. K., Knochel, A., and Müller, A. (2005). A new type of metalloprotein: The mo storage protein from Azotobacter vinelandii contains a polynuclear molybdenum-oxide cluster. CHEMBIOCHEM 6, 405-413.
Fenske, D., et al., 2005. A new type of metalloprotein: The mo storage protein from Azotobacter vinelandii contains a polynuclear molybdenum-oxide cluster. CHEMBIOCHEM, 6(2), p 405-413.
D. Fenske, et al., “A new type of metalloprotein: The mo storage protein from Azotobacter vinelandii contains a polynuclear molybdenum-oxide cluster”, CHEMBIOCHEM, vol. 6, 2005, pp. 405-413.
Fenske, D., Gnida, M., Schneider, K., Meyer-Klaucke, W., Schemberg, J., Henschel, V., Meyer, A.K., Knochel, A., Müller, A.: A new type of metalloprotein: The mo storage protein from Azotobacter vinelandii contains a polynuclear molybdenum-oxide cluster. CHEMBIOCHEM. 6, 405-413 (2005).
Fenske, Dieter, Gnida, M., Schneider, Klaus, Meyer-Klaucke, W., Schemberg, Joerg, Henschel, V., Meyer, A. K., Knochel, A., and Müller, Achim. “A new type of metalloprotein: The mo storage protein from Azotobacter vinelandii contains a polynuclear molybdenum-oxide cluster”. CHEMBIOCHEM 6.2 (2005): 405-413.

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