Structure and function of atypically coordinated enzymatic mononuclear non-heme-Fe(II) centers [0.03%]
非典型配位单核非血红素铁(II)中心的结构与功能
Daniela Buongiorno,Grit D Straganz
Daniela Buongiorno
Mononuclear, non-heme-Fe(II) centers are key structures in O2 metabolism and catalyze an impressive variety of enzymatic reactions. While most are bound via two histidines and a carboxylate, some show a different organization. A short overv...
Novel Approaches for the Accumulation of Oxygenated Intermediates to Multi-Millimolar Concentrations [0.03%]
积累氧中间体的新方法达到毫摩尔浓度
Carsten Krebs,Laura M K Dassama,Megan L Matthews et al.
Carsten Krebs et al.
Metalloenzymes that utilize molecular oxygen as a co-substrate catalyze a wide variety of chemically difficult oxidation reactions. Significant insight into the reaction mechanisms of these enzymes can be obtained by the application of a co...
Designing functional metalloproteins: from structural to catalytic metal sites [0.03%]
从结构金属位点到催化金属位点——设计功能金属蛋白
Melissa L Zastrow,Vincent L Pecoraro
Melissa L Zastrow
Metalloenzymes efficiently catalyze some of the most important and difficult reactions in nature. For many years, coordination chemists have effectively used small molecule models to understand these systems. More recently, protein design h...
X-ray absorption near-edge spectroscopy in bioinorganic chemistry: Application to M-O2 systems [0.03%]
基于X射线吸收精细结构的生物无机化学研究及其在M-O_2体系中的应用
Ritimukta Sarangi
Ritimukta Sarangi
Metal K-edge X-ray absorption spectroscopy (XAS) has been extensively applied to bioinorganic chemistry to obtain geometric structure information on metalloprotein and biomimetic model complex active sites by analyzing the higher energy ext...
CO, NO and O2 as Vibrational Probes of Heme Protein Interactions [0.03%]
一氧化碳、一氧化氮和氧气作为血红蛋白相互作用的振动探针
Thomas G Spiro,Alexandra V Soldatova,Gurusamy Balakrishnan
Thomas G Spiro
The gaseous XO molecules (X = C, N or O) bind to the heme prosthetic group of heme proteins, and thereby activate or inhibit key biological processes. These events depend on interactions of the surrounding protein with the FeXO adduct, inte...
Kinetics and thermodynamics of formation and electron-transfer reactions of Cu-O2 and Cu2-O2 complexes [0.03%]
关于Cu-O2和Cu2-O2复合物的形成及电子转移反应的动力学与热力学研究
Shunichi Fukuzumi,Kenneth D Karlin
Shunichi Fukuzumi
The kinetics and thermodynamics of formation of Cu(II)-superoxo (Cu-O2) complexes by the reaction of Cu(I) complexes with dioxygen (O2) and the reduction of Cu(II)-superoxo complexes to dinuclear Cu-peroxo complexes are discussed. In the fo...
Elizabeth C Theil,Rabindra K Behera,Takehiko Tosha
Elizabeth C Theil
Ferritins, highly symmetrical protein nanocages, are reactors for Fe2+ and dioxygen or hydrogen peroxide that are found in all kingdoms of life and in many different cells of multicellular organisms. They synthesize iron concentrates requir...
Probing oxidative stress: Small molecule fluorescent sensors of metal ions, reactive oxygen species, and thiols [0.03%]
探究氧化应激：金属离子、活性氧以及硫醇的荧光分子探针
Lynne M Hyman,Katherine J Franz
Lynne M Hyman
Oxidative stress is a common feature shared by many diseases, including neurodegenerative diseases. Factors that contribute to cellular oxidative stress include elevated levels of reactive oxygen species, diminished availability of detoxify...
Applications of pulsed EPR spectroscopy to structural studies of sulfite oxidizing enzymes() [0.03%]
脉冲EPR光谱在亚硫酸盐氧化酶结构研究中的应用()
Eric L Klein,Andrei V Astashkin,Arnold M Raitsimring et al.
Eric L Klein et al.
Sulfite oxidizing enzymes (SOEs), including sulfite oxidase (SO) and bacterial sulfite dehydrogenase (SDH), catalyze the oxidation of sulfite (SO(3) (2-)) to sulfate (SO(4) (2-)). The active sites of SO and SDH are nearly identical, each ha...
Jeffrey J Warren,Maraia E Ener,Antonín Vlček Jr et al.
Jeffrey J Warren et al.
Biological redox machines require efficient transfer of electrons and holes for function. Reactions involving multiple tunneling steps, termed "hopping," often promote charge separation within and between proteins that is essential for ener...