Primary structure of desulfoferrodoxin from Desulfovibrio desulfuricans ATCC 27774, a new class of non‐heme iron proteins

FEBS Letters

Van Beeumen, Jozef³  Tavares, Pedro¹  Devreese, Bart³  Le Gall, Jean²  Lampreia, Jorge¹  Moura, JoséJ.G.¹  Van Damme, Nancy³  Moura, Isabel¹ 

[1] Departamento de Química and Centro de Química Fina e Biotecnologia, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, Monte da Caparica, Portugal;Department of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602, USA;Vakgroep Biochemie, Fysiologie en Microbiologie, Universiteit Gent, K.L. Ledeganckstraat 35, B-9000 Gent, Belgium

关键词: Amino acid sequence;    Desulfoferrodoxin;    Rubredoxin;    Desulforedoxin;    Desulfovibrio;    Non-heme iron;    Dfx;    desulfoferrodoxin;    Dx;    desulforedoxin;    DTPA;    diethylenetriaminepentaacetic acid;   

DOI  :  10.1016/0014-5793(96)00364-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The primary structure of desulfoferrodoxin from Desulfovibrio desulfuricans ATCC 27774, a redox protein with two mononuclear iron sites, was determined by automatic Edman degradation and mass spectrometry of the composing peptides. It contains 125 amino acid residues of which five are cysteines. The first four, Cys-9, Cys-12, Cys-28 and Cys-29, are responsible for the binding of Center I which has a distorted tetrahedral sulfur coordination similar to that found in desulforedoxin from D. gigas. The remaining Cys-115 is proposed to be involved in the coordination of Center II, which is probably octahedrally coordinated with predominantly nitrogen/oxygen containing ligands as previously suggested by Mössbauer and Raman spectroscopy.

【 授权许可】

Unknown