Integrating cell-free biosyntheses of heme prosthetic group and apoenzyme for the synthesis of functional P450 monooxygenase

2012 ◽  
Vol 110 (4) ◽  
pp. 1193-1200 ◽  
Author(s):  
Yong-Chan Kwon ◽  
In-Seok Oh ◽  
Nahum Lee ◽  
Kyung-Ho Lee ◽  
Yeo Joon Yoon ◽  
...  
Keyword(s):  
Prosthetic Group ◽  
P450 Monooxygenase ◽  
Heme Prosthetic Group

Covalent Attachment of the Heme Prosthetic Group in the CYP4F Cytochrome P450 Family†

Biochemistry ◽  
2002 ◽  
Vol 41 (18) ◽  
pp. 5931-5937 ◽  
Author(s):  
Laurie A. LeBrun ◽  
Fengyun Xu ◽  
Deanna L. Kroetz ◽  
Paul R. Ortiz de Montellano
Keyword(s):  
Cytochrome P450 ◽  
Covalent Attachment ◽  
Prosthetic Group ◽  
Heme Prosthetic Group ◽  
Cytochrome P450 Family

scholarly journals Metabolism of Aminoguanidine, Diaminoguanidine, andNG-Amino-l-arginine by Neuronal NO-Synthase and Covalent Alteration of the Heme Prosthetic Group

2005 ◽  
Vol 18 (12) ◽  
pp. 1927-1933 ◽  
Author(s):  
Anthony J. Lee ◽  
Kathleen R. Noon ◽  
Suree Jianmongkol ◽  
Miranda Lau ◽  
Gary J. Jenkins ◽  
...  
Keyword(s):  
No Synthase ◽  
Prosthetic Group ◽  
Neuronal No Synthase ◽  
Heme Prosthetic Group

Effect of the Protein Matrix of Cytochromec in Suppressing the Inherent Peroxidase Activity of Its Heme Prosthetic Group

ChemBioChem ◽  
2002 ◽  
Vol 3 (1) ◽  
pp. 110-112 ◽  
Author(s):  
Rutger E. M. Diederix ◽  
Marcellus Ubbink ◽  
Gerard W. Canters
Keyword(s):  
Peroxidase Activity ◽  
Protein Matrix ◽  
Prosthetic Group ◽  
Heme Prosthetic Group

scholarly journals Control of DegP-Dependent Degradation of c-Type Cytochromes by Heme and the Cytochrome c Maturation System in Escherichia coli

2007 ◽  
Vol 189 (17) ◽  
pp. 6253-6259 ◽  
Author(s):  
Tao Gao ◽  
Mark R. O'Brian
Keyword(s):  
Escherichia Coli ◽  
Binding Motif ◽  
Dependent Manner ◽  
Heme Binding ◽  
Prosthetic Group ◽  
Cytochrome C Maturation ◽  
E Coli ◽  
Heme Prosthetic Group ◽  
Low Levels ◽  
Covalently Bound

ABSTRACT c-type cytochromes are located partially or completely in the periplasm of gram-negative bacteria, and the heme prosthetic group is covalently bound to the protein. The cytochrome c maturation (Ccm) multiprotein system is required for transport of heme to the periplasm and its covalent linkage to the peptide. Other cytochromes and hemoglobins contain a noncovalently bound heme and do not require accessory proteins for assembly. Here we show that Bradyrhizobium japonicum cytochrome c 550 polypeptide accumulation in Escherichia coli was heme dependent, with very low levels found in heme-deficient cells. However, apoproteins of the periplasmic E. coli cytochrome b 562 or the cytosolic Vitreoscilla hemoglobin (Vhb) accumulated independently of the heme status. Mutation of the heme-binding cysteines of cytochrome c 550 or the absence of Ccm also resulted in a low apoprotein level. These levels were restored in a degP mutant strain, showing that apocytochrome c 550 is degraded by the periplasmic protease DegP. Introduction of the cytochrome c heme-binding motif CXXCH into cytochrome b 562 (c-b 562) resulted in a c-type cytochrome covalently bound to heme in a Ccm-dependent manner. This variant polypeptide was stable in heme-deficient cells but was degraded by DegP in the absence of Ccm. Furthermore, a Vhb variant containing a periplasmic signal peptide and a CXXCH motif did not form a c-type cytochrome, but accumulation was Ccm dependent nonetheless. The data show that the cytochrome c heme-binding motif is an instability element and that stabilization by Ccm does not require ligation of the heme moiety to the protein.

scholarly journals The Heme Prosthetic Group of Lactoperoxidase

1998 ◽  
Vol 273 (43) ◽  
pp. 27968-27977 ◽  
Author(s):  
Tracey D. Rae ◽  
Harold M. Goff
Keyword(s):  
Prosthetic Group ◽  
Heme Prosthetic Group

Rabbit CYP4B1 engineered for high-level expression in Escherichia coli: ligand stabilization and processing of the N-terminus and heme prosthetic group

2003 ◽  
Vol 416 (1) ◽  
pp. 17-24 ◽  
Author(s):  
Matthew J Cheesman ◽  
Brian R Baer ◽  
Yi-Min Zheng ◽  
Elizabeth M.J Gillam ◽  
Allan E Rettie
Keyword(s):  
Escherichia Coli ◽  
High Level Expression ◽  
Prosthetic Group ◽  
Expression In Escherichia Coli ◽  
N Terminus ◽  
Ligand Stabilization ◽  
Heme Prosthetic Group ◽  
High Level

Improvements in the isolation procedure for thyroid peroxidase: Nature of the heme prosthetic group

1970 ◽  
Vol 139 (1) ◽  
pp. 221-229 ◽  
Author(s):  
Alvin Taurog ◽  
Martha L. Lothrop ◽  
Ronald W. Estabrook
Keyword(s):  
Isolation Procedure ◽  
Thyroid Peroxidase ◽  
Prosthetic Group ◽  
Heme Prosthetic Group
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