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The Chlamydomonas reinhardtii MoCo carrier protein is multimeric and stabilizes molybdopteria cofactor in a molybdate charged form

Publikation: Beitrag in FachzeitschriftArtikelForschungPeer-Review

Autorschaft

  • Claus Peter Witte
  • M. Isabel Igeño
  • Ralf Mendel
  • Günter Schwarz

Externe Organisationen

  • The James Hutton Institute
  • Universidad de Cordoba
  • Technische Universität Braunschweig

Details

OriginalspracheEnglisch
Seiten (von - bis)205-209
Seitenumfang5
FachzeitschriftFEBS letters
Jahrgang431
Ausgabenummer2
PublikationsstatusVeröffentlicht - 17 Juli 1998
Extern publiziertJa

Abstract

In Chlamydomonas reinhardtii, molybdopterin cofactar (MoCo) able to reconstitute active nitrate reductase (NR) with apoenzyme from the Neurospora crassa mutant nit-1 was found mostly bound to a carrier protein (CP). This protein is scarce in the algal free extracts and has been purified 520-fold. MoCoCP is a protein of 64 kDa with subunits of 16.5 kDa and an isoelectric point of 4.5. In contrast to free MoCo, MoCo bound to CP was remarkably protected against inactivation under both aerobic conditions and basic pH. MocoCP transferred active MoCo to apoNR in vitro without addition of molybdate, though reconstituted activity was 20% higher in the presence of molybdate. Incubation with tungstate specifically inhibited MoCoCP activity but had no effect an the activity of free MoCo released from milk xanthine oxidase. MoCoCP did not charge molybdate unless in the presence of N. crassa extracts. Our data support that MoCoCP stabilizes MoCo in an active form charged with molybdate to provide MoCo to apomolybdoenzymes.

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The Chlamydomonas reinhardtii MoCo carrier protein is multimeric and stabilizes molybdopteria cofactor in a molybdate charged form. / Witte, Claus Peter; Igeño, M. Isabel; Mendel, Ralf et al.
in: FEBS letters, Jahrgang 431, Nr. 2, 17.07.1998, S. 205-209.

Publikation: Beitrag in FachzeitschriftArtikelForschungPeer-Review

Witte CP, Igeño MI, Mendel R, Schwarz G, Fernández E. The Chlamydomonas reinhardtii MoCo carrier protein is multimeric and stabilizes molybdopteria cofactor in a molybdate charged form. FEBS letters. 1998 Jul 17;431(2):205-209. doi: 10.1016/S0014-5793(98)00756-X
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abstract = "In Chlamydomonas reinhardtii, molybdopterin cofactar (MoCo) able to reconstitute active nitrate reductase (NR) with apoenzyme from the Neurospora crassa mutant nit-1 was found mostly bound to a carrier protein (CP). This protein is scarce in the algal free extracts and has been purified 520-fold. MoCoCP is a protein of 64 kDa with subunits of 16.5 kDa and an isoelectric point of 4.5. In contrast to free MoCo, MoCo bound to CP was remarkably protected against inactivation under both aerobic conditions and basic pH. MocoCP transferred active MoCo to apoNR in vitro without addition of molybdate, though reconstituted activity was 20% higher in the presence of molybdate. Incubation with tungstate specifically inhibited MoCoCP activity but had no effect an the activity of free MoCo released from milk xanthine oxidase. MoCoCP did not charge molybdate unless in the presence of N. crassa extracts. Our data support that MoCoCP stabilizes MoCo in an active form charged with molybdate to provide MoCo to apomolybdoenzymes.",
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AU - Witte, Claus Peter

AU - Igeño, M. Isabel

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AU - Schwarz, Günter

AU - Fernández, Emilio

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N2 - In Chlamydomonas reinhardtii, molybdopterin cofactar (MoCo) able to reconstitute active nitrate reductase (NR) with apoenzyme from the Neurospora crassa mutant nit-1 was found mostly bound to a carrier protein (CP). This protein is scarce in the algal free extracts and has been purified 520-fold. MoCoCP is a protein of 64 kDa with subunits of 16.5 kDa and an isoelectric point of 4.5. In contrast to free MoCo, MoCo bound to CP was remarkably protected against inactivation under both aerobic conditions and basic pH. MocoCP transferred active MoCo to apoNR in vitro without addition of molybdate, though reconstituted activity was 20% higher in the presence of molybdate. Incubation with tungstate specifically inhibited MoCoCP activity but had no effect an the activity of free MoCo released from milk xanthine oxidase. MoCoCP did not charge molybdate unless in the presence of N. crassa extracts. Our data support that MoCoCP stabilizes MoCo in an active form charged with molybdate to provide MoCo to apomolybdoenzymes.

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