Structural reorganization renders enhanced metalloprotein stability

被引：1

作者：

Botelho, Hugo M. ^{[1
]}

Gomes, Claudio M. ^{[1
]}

机构：

[1] Univ Nova Lisboa, Inst Tecnol Quim & Biol, EAN, P-2785572 Oeiras, Portugal

来源：

CHEMICAL COMMUNICATIONS | 2011年 / 47卷 / 39期

关键词：

DESULFOVIBRIO-GIGAS RUBREDOXIN; CLOSTRIDIUM-PASTEURIANUM; MESOPHILIC RUBREDOXIN; CIRCULAR-DICHROISM; NMR STRUCTURE; PROTEINS; RESOLUTION; DYNAMICS; MODEL;

D O I：

10.1039/c1cc13354c

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

The enhanced stability of a mesophilic metalloprotein was assessed using biophysical spectroscopies. Significant local structural inter-conversions during thermal insult account for a reorganization of the protein scaffold, without disturbing the active metal site. This cushioning mechanism is proposed to be a generic property of metalloproteins contributing to enhanced stability.

引用

页码：11149 / 11151

页数：3

共 20 条

[11] How to study proteins by circular dichroism [J].

Kelly, SM ;

Jess, TJ ;

Price, NC .

BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, 2005, 1751 (02) :119-139

[12] NMR structure of Desulfovibrio gigas rubredoxin:: a model for studying protein stabilization by compatible solutes [J].

Lamosa, P ;

Brennan, L ;

Vis, H ;

Turner, DL ;

Santos, H .

EXTREMOPHILES, 2001, 5 (05) :303-311

[13]

Lazaridis T, 1997, PROTEIN SCI, V6, P2589

[14] Miniaturized metalloproteins: Application to iron-sulfur proteins [J].

Lombardi, A ;

Marasco, D ;

Maglio, O ;

Di Costanzo, L ;

Nasti, F ;

Pavone, V .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2000, 97 (22) :11922-11927

[15] RUBREDOXIN - A NEW ELECTRON TRANSFER PROTEIN FROM CLOSTRIDIUM PASTEURIANUM [J].

LOVENBERG, W ;

SOBEL, BE .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1965, 54 (01) :193-+

[16] Iron-Nucleated Folding of a Metalloprotein in High Urea: Resolution of Metal Binding and Protein Folding Events [J].

Morleo, Anna ;

Bonomi, Francesco ;

Iametti, Stefania ;

Huang, Victor W. ;

Kurtz, Donald M., Jr. .

BIOCHEMISTRY, 2010, 49 (31) :6627-6634

[17] Femtomolar Zn(II) affinity in a peptide-based ligand designed to model thiolate-rich metalloprotein active sites [J].

Petros, Amy K. ;

Reddi, Amit R. ;

Kennedy, Michelle L. ;

Hyslop, Alison G. ;

Gibney, Brian R. .

INORGANIC CHEMISTRY, 2006, 45 (25) :9941-9958

[18] Contact order, transition state placement and the refolding rates of single domain proteins [J].

Plaxco, KW ;

Simons, KT ;

Baker, D .

JOURNAL OF MOLECULAR BIOLOGY, 1998, 277 (04) :985-994

[19] ESTABLISHING ISOSTRUCTURAL METAL SUBSTITUTION IN METALLOPROTEINS USING H-1-NMR, CIRCULAR-DICHROISM, AND FOURIER-TRANSFORM INFRARED-SPECTROSCOPY [J].

POUNTNEY, DL ;

HENEHAN, CJ ;

VASAK, M .

PROTEIN SCIENCE, 1995, 4 (08) :1571-1576

[20] Hyperthermophilic enzymes: Sources, uses, and molecular mechanisms for thermostability [J].

Vieille, C ;

Zeikus, GJ .

MICROBIOLOGY AND MOLECULAR BIOLOGY REVIEWS, 2001, 65 (01) :1-+

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