Mössbauer Studies on the Iron-ligand Binding in Hemoproteins and Their Related Compounds

نویسنده

  • Y. Maeda
چکیده

The electronic structure of the heme iron in hemoproteins is characterized by its changeable valence and spin states. These features are discussed in hemoproteins and their related model compounds. The iron-ligand binding, especially the reversible dioxygen binding in myoglobin and hemoglobin is discussed in details by using the f4;issbauer spectroscopic knowledge obtained from the experiments with Mb single crystals and model compounds. A comparison of recent experimental evidences with calculations has improved the knowledge of the iron-dioxygen binding structure. The electronic structures in the deoxygenated state and the CO compound are also deduced. In addition, kinetics of ligand-binding to hemoproteins is reported.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

In-silico Investigation of Tubulin Binding Modes of a Series of Novel Antiproliferative Spiroisoxazoline Compounds Using Docking Studies

Interference with microtubule polymerization results in cell cycle arrest leading to cell death. Colchicine is a well-known microtubule polymerization inhibitor which does so by binding to a specific site on tubulin. A set of 3',4'-bis (substituted phenyl)-4'H-spiro[indene-2,5'-isoxazol]-1(3H)-one derivatives with known antiproliferative activities were evaluated for their tubulin binding modes...

متن کامل

Electromagnetic Properties of Hemoproteins III. ELECTRON PARAMAGNETIC RESONANCE CHARACTERISTICS OF IRON (III) AND MANGANESE (II) PROTOPORPHYRINS IX AND THEIR APOHEMOPROTEIN COMPLEXES IN HIGH SPIN STATES*

Manganese protoporphyrin IX was recombined with apoproteins of cytochrome c peroxidase, horseradish peroxidase, myoglobin, and hemoglobin to prepare artificial hemoproteins containing the manganese porphyrin in place of protoheme or iron protoporphyrin IX. Electron paramagnetic resonance (EPR) spectra of manganese (II) protoporphyrin IX and its apohemoprotein complexes were measured at Xand K-b...

متن کامل

In-silico Investigation of Tubulin Binding Modes of a Series of Novel Antiproliferative Spiroisoxazoline Compounds Using Docking Studies

Interference with microtubule polymerization results in cell cycle arrest leading to cell death. Colchicine is a well-known microtubule polymerization inhibitor which does so by binding to a specific site on tubulin. A set of 3',4'-bis (substituted phenyl)-4'H-spiro[indene-2,5'-isoxazol]-1(3H)-one derivatives with known antiproliferative activities were evaluated for their tubulin binding modes...

متن کامل

Molecular Modeling Studies on Vinblastine Binding Site of Tubulin for Antimitotic agents

Medicinal chemistry depends on many other disciplines ranging from organic chemistry andpharmacology to computational chemistry. Typically medicinal chemists use the moststraightforward ways to prepare compounds. The validation of any design project comes from thebiological testing.Studies of the binding site of vinblastine by a single cross—linking experiment identified it asbeing between resi...

متن کامل

Studies on Nickel(II)-Pyridoxamine-Imidazole Containing Mixed Ligand Complex Systems

The stability constants of species present in the systems Ni(II)-pyridoxamine(pym)(A) and Ni(II)-pyridoxamine(pym)(A)-imidazole containing ligands(B) [B = imidazole(him),  benzimidazole(bim), histamine(hist) and L-histidine(his)] have been determined pH-metrically using the MINIQUAD computer program. The existence of the species NiAH, NiA and NiA2 was proven for the Ni(II)-pym(A)...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:

دوره   شماره 

صفحات  -

تاریخ انتشار 2016