Articles written in Journal of Chemical Sciences
Volume 93 Issue 3 April 1984 pp 295-311 Structural Chemistry
Nuclear magnetic resonance of paramagnetic metalloporphyrins
The present article reviews and discusses proton magnetic resonance studies on metalloporphyrins which provide good models for heme proteins in their physical and chemical properties. Emphasis is given on the discussion of the1H
Volume 95 Issue 1-2 July 1985 pp 189-205
Electronic structure of spin-mixed iron(III) porphyrins: A proton magnetic resonance study
L B Dugad V R Marathe Samaresh Mitra
The proton magnetic resonance studies on the perchlorato iron(III) porphyrins in solution have been described. The isotropic proton shifts in these complexes show anomalous temperature dependence, consistent with its unusual properties in solid state. The
Volume 98 Issue 1-2 January 1987 pp 53-68
Low temperature high field magnetisation studies on metalloporphyrins
Magnetisation studies at very high magnetic fields and low temperatures on several high-spin iron (III) and manganese (III) porphyrins are reviewed. The usefulness of these studies in understanding the properties of the ground electronic state of the metal ion is discussed.
Volume 102 Issue 3 June 1990 pp 193-193
Volume 102 Issue 3 June 1990 pp 418-462
Abstracts of posters presented at the symposium
Bhaskar G Maiya S M S Chauhan P Bhyrappa V Krishnan P K Bhardwaj Sabyasachi Sarkar Krishna B Pandeya Pavan Mathur Akhil R Chakravarty Birinchi K Das Digambar V Behere Sandeep Modi Samaresh Mitra Sandeep Modi Digambar V Behere Samaresh Mitra Anil Saxena Sandeep Modi Digambar V Behere S Mitra Shyamalava Mazumdar Okhil K Medhi Samaresh Mitra Shyamalava Mazumdar Samaresh Mitra Anup Madan Sandeep Modi Anil Saxena Digamber V Behere S Mitra T Pandiyan M Palaniandavar K L Narayanan H Manohar R Ramaraj C C Thomas S Rajagopal T Rajendra C Srinivasan P Ramamurthy R Roy M C Saha S Panchanan P S Roy C Balagopalakrishna M V Rajasekharan B V Agarwala S Hingorani G A Nagena Gowda Y S Ramaswamy R Halesha N M N Gowda G K N Reddy G C Saxena K L Gupta P Srivastava V D Gupta M Ray R N Mukherjee R N Mohanty K C Dash Ramesh Kapoor S Yadav V Sood P Kapoor B N Anand R Bains Usha K Aggarwal P Garge R Chikate S Padhye J M Savariault P De Loth J P Tuchgues V K Jain M A Vaidya S C Jain S Kalyan Kumar Harkesh B Singh K M Mangaonkar D N Patkar N K Jha Pankaj Sharma S K Date C E Deshpande S D Sathaye S B Deshpande H S Potdar V S Darshane A C Dash R K Nanda N N Das S Gangopadhyay P Banerjee S K Kulshreshtha P S Zacharias N Arulsamy T Ramasami V Subramanian B U Nair M Kanthimathi G Sundararajan V Shivasubramanian R G Bhattacharya S Biswas J Armstrong E M Holt A P Koley
Volume 106 Issue 1 February 1994 pp 29-35 Inorganic and Analytical
Inhibition of oxidoreductase activity of xanthine oxidase by Cu2+ and Hg2+ ions
Madhu Sudan Mondal Digambar V Behere Samaresh Mitra
Xanthine oxidase has been isolated in good yield and pure form. Inhibition of the enzyme by Cu2+ and Hg2+ ions has been studied. The nature and extent of the inhibition have been determined.
Volume 106 Issue 3 June 1994 pp 729-734
Stereochemical structure and biochemical activity of heme proteins
A correlation between the stereochemical geometry around the metal ion in heme enzymes and their catalytic properties is attempted. It is shown that spin-lattice relaxation time measurement of bulk water in the enzyme solution gives accurate information as to the presence or absence of water molecule at the sixth coordination site of the heme iron. The rate of formation of compound I, an intermediate in the catalytic cycle of the enzymes, is shown to be directly related to the nature of the sixth coordination site of the heme.
Volume 106 Issue 3 June 1994 pp 763-763
Miceile-induced release of heme-NO from nitric oxide complex of myogiobin
Volume 106 Issue 3 June 1994 pp 767-767
Interaction of metal ions on the transient reductive half reaction of xanthine oxidase
Volume 107 Issue 4 August 1995 pp 497-503
Heme CD as a probe for monitoring local structural changes in hemeproteins: Alkaline transition in hemeproteins
Tapan K Das Shyamalava Mazumdar Samaresh Mitra
Structural change due to acid-alkaline transition in hemeproteins were monitored by circular dichroism measurements in the Soret region. It was observed that in cytochrome c and horseradish peroxidase, alkaline transition results in a large change in the heme CD due to significant conformational change in the heme cavity region. In metmyoglobin a simple protolytic mechanism associated with alkaline transition involves very small conformational changes.
Volume 108 Issue 3 June 1996 pp 313-313 Modern Trends In Inorganic Chemistry
Protein-surfactant interaction: Selective unfolding in hemeproteins
Volume 111 Issue 3 June 1999 pp 501-508 Modern Trends In Inorganic Chemistry
Altered redox affinity of xanthine oxidase active sites by copper(II) ions
Madhu Sudan Mondal Samaresh Mitra
The interaction of Cu2+ ion with the redox centres of xanthine oxidase (XO) has been investigated using optical difference spectroscopic measurements. Anaerobic enzyme-reduction experiments using controlled and excess substrates (xanthine and NADH) have been performed to investigate the perturbation of XO active sites in the presence of Cu2+ ions. The results indicate an overall alteration in the redox affinities (i.e. affinity to accept electrons) of the active sites of XO by Cu2+ ion.
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