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OXYGEN UTILIZING MEMBRANE HEME PROTEINS

利用膜血红素蛋白供氧

基本信息

批准号：
6519864
负责人：
SHELAGH M FERGUSON-MILLER
金额：
$ 90.48万
依托单位：
MICHIGAN STATE UNIVERSITY
依托单位国家：
美国
项目类别：
财政年份：
1998
资助国家：
美国
起止时间：
1998-06-01 至 2004-05-31
项目状态：
已结题

来源：
https://reporter.nih.gov/project-details/6519864
关键词：
chemical transfer reaction cytochrome c cytochrome oxidase enzyme structure hemoprotein membrane proteins oxidation prostaglandin endoperoxide synthase

项目摘要

The goal of this Program Project entitled Oxygen Utilizing Membrane Heme Proteins is to characterize the structures of prostaglandin H synthases (GHSs) and cytochrome c oxidase (CcOX) in the context of the chemical changes that occur during catalysis as these enzymes interact with their substrates and with biological membranes. PGHS catalyzes the initial step in the biosynthesis of prostanoids--the formation of prostaglandin endoperoxide H2 from arachidonic acid, two molecules of 02 and two electrons. CcOX is a terminal heme/Cu oxidase of the respiratory electron- transfer chain which catalyzes a net four electron reduction of 02 to two H20 molecules with concomitant translocation of four protons across the mitochondrial inner membrane (or bacterial plasma membrane). There are five projects and four cores. Project I: Cyclooxygenase Catalysis and Suicide Inactivation (Smith) will examine the binding of arachidonate to the cyclooxygenase site of PGHS, the mechanism of suicide inactivation and the role of H20 channels in PGHS. Project II: Structural Biology of Peroxidation by PGH Synthases (Garavito) will examine the structural aspects of peroxidase catalysis in PGHSs and discern the structural basis for the differences in the peroxidative activities of PGHS-1 and -2. Project III: Monotopic Membrane Anchors in PGH Synthases-1 and -2 (DeWitt) will test the hypothesis that PGHS-1 and PGHS-2 associate with a single leaflet of the membrane bilayer through hydrophobic faces of four contiguous amphipathic helices present in the amino-terminal third of the proteins. Project IV: Substrate Docking in Cytochrome c resolved Spectroscopy of Cytochrome Oxidases and PGH Synthases (Babcock) is designed to understand oxygen and peroxide activation by CcOX and PGHSs and the mechanisms by which the free energy is released in the reduction of these substrates. Core A. Administration (Smith), Core B: Membrane Protein Expression and Purification (DeWitt), Core C: Crystallization and X-ray Crystallography (Garavito) and Core D: EPR and Resonance Raman Spectroscopy (McCracken) provide administrative and technical support for these projects.

这个项目的目标是“氧气利用膜血红素”

项目成果

期刊论文数量（17）

专著数量（0）

科研奖励数量（0）

会议论文数量（0）

专利数量（0）

Histidine 386 and its role in cyclooxygenase and peroxidase catalysis by prostaglandin-endoperoxide H synthases.

组氨酸 386 及其在前列腺素内过氧化物 H 合酶催化环氧合酶和过氧化物酶中的作用。

DOI：
10.1074/jbc.m306319200
发表时间：
2003
期刊：
The Journal of biological chemistry
影响因子：
0
作者：
Seibold,SteveA;Ball,Terry;Hsi,LindaC;Mills,DeniseA;Abeysinghe,RajeewaD;Micielli,Renee;Rieke,CarolineJill;Cukier,RobertI;Smith,WilliamL
通讯作者：
Smith,WilliamL

An arginine to lysine mutation in the vicinity of the heme propionates affects the redox potentials of the hemes and associated electron and proton transfer in cytochrome c oxidase.

丙酸血红素附近的精氨酸到赖氨酸的突变影响血红素的氧化还原电位以及细胞色素c氧化酶中相关的电子和质子转移。

DOI：
10.1021/bi050283d
发表时间：
2005
期刊：
Biochemistry
影响因子：
2.9
作者：
Mills,DeniseA;Geren,Lois;Hiser,Carrie;Schmidt,Bryan;Durham,Bill;Millett,Francis;Ferguson-Miller,Shelagh
通讯作者：
Ferguson-Miller,Shelagh

Different catalytically competent arrangements of arachidonic acid within the cyclooxygenase active site of prostaglandin endoperoxide H synthase-1 lead to the formation of different oxygenated products.

前列腺素内过氧化物 H 合酶 1 环加氧酶活性位点内花生四烯酸的不同催化能力排列导致不同氧化产物的形成。