Characterization of a partially unfolded high potential iron protein

被引：66
作者：
Bertini, I
Cowan, JA
Luchinat, C
Natarajan, K
Piccioli, M
机构：
[1] OHIO STATE UNIV, DEPT CHEM, EVANS LAB CHEM, COLUMBUS, OH 43210 USA
[2] UNIV FLORENCE, DEPT SOIL CHEM & PLANT NUTR, I-50144 FLORENCE, ITALY
来源：
BIOCHEMISTRY | 1997年 / 36卷 / 31期
关键词：
D O I：
10.1021/bi970810w
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
A partially unfolded state of the Fe4S4-containing high potential iron-sulfur protein from Chromatium vinosum has been detected and characterized by NMR spectroscopy following addition of a concentrated solution of guanidinium chloride to the native protein. This intermediate species (i) maintains the polymetallic center, (ii) exhibits a largely collapsed secondary structure, and (iii) undergoes East cluster decomposition upon oxidation. This information is framed into the knowledge about this class of proteins, and the possible role of this intermediate with respect to the in vivo folding/unfolding process is discussed as well its role in the slow hydrolytic degradation characteristic of oxidized HiPIPs.
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页码：9332 / 9339
页数：8
相关论文
共 68 条
[1]   SYNTHESIS, CLONING AND EXPRESSION OF A SYNTHETIC GENE FOR HIGH-POTENTIAL IRON PROTEIN FROM CHROMATIUM-VINOSUM [J].
AGARWAL, A ;
TAN, J ;
EREN, M ;
TEVELEV, A ;
LUI, SM ;
COWAN, JA .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1993, 197 (03) :1357-1362
[2]   ROLE OF AROMATIC RESIDUES IN STABILIZATION OF THE [FE4S4] CLUSTER IN HIGH-POTENTIAL IRON PROTEINS (HIPIPS) - PHYSICAL CHARACTERIZATION AND STABILITY STUDIES OF TYR-19 MUTANTS OF CHROMATIUM-VINOSUM HIPIP [J].
AGARWAL, A ;
LI, DW ;
COWAN, JA .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1995, 92 (21) :9440-9444
[3]   Influence of oxygen ligation on [Fe4S4] cluster properties. Characterization of the Cys77Ser mutant of Chromatium vinosum HiPIP [J].
Agarwal, A ;
Li, DW ;
Cowan, JA .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1996, 118 (04) :927-928
[4]   A COMPARISON OF THE PH, UREA, AND TEMPERATURE-DENATURED STATES OF BARNASE BY HETERONUCLEAR NMR - IMPLICATIONS FOR THE INITIATION OF PROTEIN-FOLDING [J].
ARCUS, VL ;
VUILLEUMIER, S ;
FREUND, SMV ;
BYCROFT, M ;
FERSHT, AR .
JOURNAL OF MOLECULAR BIOLOGY, 1995, 254 (02) :305-321
[5]   A serine->cysteine ligand mutation in the high potential iron-sulfur protein from Chromatium vinosum provides insight into the electronic structure of the [4Fe-4S] cluster [J].
Babini, E ;
Bertini, I ;
Borsari, M ;
Capozzi, F ;
Dikiy, A ;
Eltis, LD ;
Luchinat, C .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1996, 118 (01) :75-80
[6]   H-1 NOE STUDIES ON DICOPPER(II) DICOBALT(II) SUPEROXIDE-DISMUTASE [J].
BANCI, L ;
BERTINI, I ;
LUCHINAT, C ;
PICCIOLI, M ;
SCOZZAFAVA, A ;
TURANO, P .
INORGANIC CHEMISTRY, 1989, 28 (26) :4650-4656
[7]   THE 3-DIMENSIONAL SOLUTION STRUCTURE OF THE REDUCED HIGH-POTENTIAL IRON-SULFUR PROTEIN FROM CHROMATIUM-VINOSUM THROUGH NMR [J].
BANCI, L ;
BERTINI, I ;
DIKIY, A ;
KASTRAU, DHW ;
LUCHINAT, C ;
SOMPORNPISUT, P .
BIOCHEMISTRY, 1995, 34 (01) :206-219
[8]   THE 3-DIMENSIONAL STRUCTURE IN SOLUTION OF THE PARAMAGNETIC HIGH-POTENTIAL IRON-SULFUR PROTEIN-I FROM ECTOTHIORHODOSPIRA-HALOPHILA THROUGH NUCLEAR-MAGNETIC-RESONANCE [J].
BANCI, L ;
BERTINI, I ;
ELTIS, LD ;
FELLI, IC ;
KASTRAU, DHW ;
LUCHINAT, C ;
PICCIOLI, M ;
PIERATTELLI, R ;
SMITH, M .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1994, 225 (02) :715-725
[9]   BACKBONE DYNAMICS OF CALMODULIN STUDIED BY N-15 RELAXATION USING INVERSE DETECTED 2-DIMENSIONAL NMR-SPECTROSCOPY - THE CENTRAL HELIX IS FLEXIBLE [J].
BARBATO, G ;
IKURA, M ;
KAY, LE ;
PASTOR, RW ;
BAX, A .
BIOCHEMISTRY, 1992, 31 (23) :5269-5278
[10]   RECENT DEVELOPMENTS IN THE FIELD OF IRON-SULFUR PROTEINS [J].
BEINERT, H .
FASEB JOURNAL, 1990, 4 (08) :2483-2491
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