International Year of Chemistry, 2011

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International Year of Chemistry 2011

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Bioinorganic Chem

Special issue of the Indian Journal of Chemistry, Section A

A collection of 25 articles at the interface of inorganic chemistry and biology makes up this special issue of the Indian Journal of Chemistry Section A. Produced in celebration of IYC2011, this special issue on bioinorganic chemistry bears special significance since it recognizes this as a frontier area of research in the 21st century.

“The field of bioinorganic chemistry is booming, with investigators all the way from the most fundamental areas of physics and chemistry to some of the most exciting areas of biology and medicine”, writes Harry Gray in the foreword to this issue. “The stars of the issue of course are metals, with emphasis on molybdenum, iron, and copper, but also including calcium and a few key lanthanides. There are outstanding papers on protein structure function relationships, probes of structure and dynamics, metal transport, biomimetic model systems, theoretical formulations of the structures of active sites, and the photochemistry of DNA.”

Five of the articles are thematic reviews that cover bioinorganic chemistry, including the biogenesis of cytochrome c oxidase, xanthine oxidase, metal-phenolates, and, CO and O2 binding and activation, etc. The remaining are original research papers.

IJC-A Vol.50A(03-04) [March-April 2011]
Guest Editors: Shyamalava Mazumdar, Rabindranath Mukherjee, and Chebrolu Pulla Rao
available online http://nopr.niscair.res.in/handle/123456789/11213

nanocage
(left) Image from Suranjana Haldar, Takehiko Tosha, and Elizabeth C Theil, ‘Moving iron in ferritin: Leucine 154, a residue near Fe(III) during mineral buildup minimizes mineral dissolution’, p. 414.
Mineral dissolution from eukaryotic ferritin protein nanocages is influenced by conserved residue leucine 154. The residue (illustrated in red) is identified by proximity to ferric oxo mineral nuclei by NMR; view from the inside of the ferritin protein cage (yellow polypeptide helices). Each L154 residue is at the entry to the mineralization cavity, ~ 60% of the protein cage volume, from each of the 24-subunit nucleation channels, and, because of cage geometry, in a group of four L154 residues around the fourfold axes of the cage.

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featured Apr 20, 2011