Current understanding of the function of magnesium chelatase

被引：30

作者：

Reid, JD ^{[1
]}

Hunter, CN ^{[1
]}

机构：

[1] Univ Sheffield, Dept Mol Biol & Biotechnol, Sheffield S10 2TN, S Yorkshire, England

来源：

BIOCHEMICAL SOCIETY TRANSACTIONS | 2002年 / 30卷

关键词：

AAAATPase; chlorophyll biosynthesis; I/D/H subunits; porphyrin; tetrapyrrole;

D O I：

10.1042/bst0300643

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：

Despite the global significance of chlorophylls and other modified tetrapyrroles, many aspects of their biosynthetic pathways are poorly understood. A y key enzyme at the branch point between the haem and chlorophyll pathways, magnesium chelatase, couples the free energy of ATP hydrolysis to the insertion of magnesium into porphyrin, a process that is likely to be mediated through protein conformational changes. Conclusions from recent structural and functional studies of individual subunits are combined to provide a mechanistic outline of the full magnesium chelatase complex. Gathering further information presents a considerable challenge, and recent steps towards this goal will be introduced.

引用

页码：643 / 645

页数：3

共 18 条

[1] Resonance Raman spectra of ferrochelatase reveal porphyrin distortion upon metal binding [J].

Blackwood, ME ;

Rush, TS ;

Medlock, A ;

Dailey, HA ;

Spiro, TG .

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1997, 119 (50) :12170-12174

[2] Magnesium chelatase from Rhodobacter sphaeroides:: initial characterization of the enzyme using purified subunits and evidence for a BchI-BchD complex [J].

Gibson, LCD ;

Jensen, PE ;

Hunter, CN .

BIOCHEMICAL JOURNAL, 1999, 337 :243-251

[3] MAGNESIUM-PROTOPORPHYRIN CHELATASE OF RHODOBACTER-SPHAEROIDES - RECONSTITUTION OF ACTIVITY BY COMBINING THE PRODUCTS OF THE BCHH, BCHI, AND BCHD GENES EXPRESSED IN ESCHERICHIA-COLI [J].

GIBSON, LCD ;

WILLOWS, RD ;

KANNANGARA, CG ;

VON WETTSTEIN, D ;

HUNTER, CN .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1995, 92 (06) :1941-1944

[4] A putative Mg chelatase subunit from Arabidopsis thaliana cv C24 - Sequence and transcript analysis of the gene, import of the protein into chloroplasts, and in situ localization of the transcript and protein [J].

Gibson, LCD ;

Marrison, JL ;

Leech, RM ;

Jensen, PE ;

Bassham, DC ;

Gibson, M ;

Hunter, CN .

PLANT PHYSIOLOGY, 1996, 111 (01) :61-71

[5] Mg-chelatase of tobacco:: The role of the subunit CHL D in the chelation step of protoporphyrin IX [J].

Gräfe, S ;

Saluz, HP ;

Grimm, B ;

Hänel, F .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1999, 96 (05) :1941-1946

[6] Modification of cysteine residues in the ChlI and ChlH subunits of magnesium chelatase results in enzyme inactivation [J].

Jensen, PE ;

Reid, JD ;

Hunter, CN .

BIOCHEMICAL JOURNAL, 2000, 352 :435-441

[7] ATPase activity associated with the magnesium-protoporphyrin IX chelatase enzyme of Synechocystis PCC6803:: evidence for ATP hydrolysis during Mg2+ insertion, and the MgATP-dependent interaction of the ChlI and ChlD subunits [J].

Jensen, PE ;

Gibson, LCD ;

Hunter, CN .

BIOCHEMICAL JOURNAL, 1999, 339 :127-134

[8] Determinants of catalytic activity with the use of purified I, D and H subunits of the magnesium protoporphyrin IX chelatase from Synechocystis PCC6803 [J].

Jensen, PE ;

Gibson, LCD ;

Hunter, CN .

BIOCHEMICAL JOURNAL, 1998, 334 :335-344

[9] Expression of the chlI, chlD, and chlH genes from the cyanobacterium Synechocystis PCC6803 in Escherichia coli and demonstration that the three cognate proteins are required for magnesium-protoporphyrin chelatase activity [J].

Jensen, PE ;

Gibson, LCD ;

Henningsen, KW ;

Hunter, CN .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1996, 271 (28) :16662-16667

[10]

Jensen PE, 1996, MOL GEN GENET, V250, P383

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