Titlebook: Metal Sites in Proteins and Models; Iron Centres H. A. O. Hill,P. J. Sadler,A. J. Thomson Book 1997 Springer-Verlag Berlin Heidelberg 1997

Antioxidant

省略

GENUS

Nick E. Le Brun,Andrew J. Thomson,Geoffrey R. Moore

Itinerant

Luet-Lok Wong,Andrew C. G. Westlake,Darren P. Nickerson

開始發(fā)作

藕床生厭倦

Polyiron oxides, oxyhydroxides and hydroxides as models for biomineralisation processes,the lithosphere, but some of which, such as the mineral found within the iron storage protein ferritin, are metastable. This article takes the specific example of loaded ferritin as a biomineral and explores the use of model compounds to elucidate the formation, structure and properties of the iron

micturition

Heme: The most versatile redox centre in biology?,ical functions. These include: Simple electron transfer reactions, oxygen transport and storage, oxygen reduction to the level of hydrogen peroxide or water, oxygenations of organic substrates, and the reduction of peroxides. This diversity of function is often extended further by combining heme gro

審問,審訊

Rationalisation of metal binding to transferrin: Prediction of metal-protein stability constants,for the study of the differences between the two metal binding sites (the N- and C-lobe sites), and mechanisms for the uptake and release of both metal ions and synergistic anions are discussed. The strength of metal binding to transferrin can be rationalised on the basis of metal ion acidity (stren

山崩

Metal centres of bacterioferritins or non-haem-iron-containing cytochromes ,, ,ember of the ferritin family of proteins and thus is also called bacterioferritin. It consists of 24 polypeptide subunits and, in addition to its inter-subunit bis-methionine coordinated haem b groups, it also contains intra-subunit dinuclear metal centres and has the capacity for a central non-haem

Medicaid

,Ribonucleotide reductases — a group of enzymes with different metallosites and a similar reaction mintricate allosteric regulation enables one and the same enzymic component to accept both purine and pyrimidine ribonucleotide substrates and to furnish growing cells with balanced deoxyribonucleotide pools. The reaction, which is based on radical chemistry, is common to all ribonucleotide reductase