[4] Circular dichroism

RW Woody - Methods in enzymology, 1995 - Elsevier
Publisher Summary Circular dichroism (CD) is a spectroscopic method which depends on
the fact that certain molecules interact differently with right and left circularly polarized light …

Structure and function of haemoglobin

JM Baldwin - Progress in biophysics and molecular biology, 1976 - Elsevier
Haemoglobin is the respiratory protein in the red blood cells of vertebrates. Its physiological
functions are to transport oxygen from the lungs to the tissues and to facilitate the transport of …

[图书][B] Porphyrins and metalloporphyrins

KM Smith - 1975 - core.ac.uk
In 1964, JE Falk was able to give one man's view of the porphyrinand metalloporphyrin field
at possibly the last time that such a major task was possible. Since then the area has …

[图书][B] The Porphyrins V7: Biochemistry, Part B

D Dolphin - 2012 - books.google.com
The Porphyrins, Volume VII: Biochemistry, Part B is devoted to the biochemistry of
porphyrins, their precursors, and related compounds. The book covers the structure and …

Stereochemistry of cooperative mechanisms in hemoglobin

MF Perutz, G Fermi, B Luisi, B Shaanan… - Accounts of Chemical …, 1987 - ACS Publications
Hemoglobin (Hb) is the respiratory protein of the red blood cells which carries 02 from the
lungs to the tissues and facilitates the return transport of C02 from the tissues to the lungs …

Heme-based sensors, exemplified by the kinase FixL, are a new class of heme protein with distinctive ligand binding and autoxidation

MA Gilles-Gonzalez, G Gonzalez, MF Perutz… - Biochemistry, 1994 - ACS Publications
Revised Manuscript Received May 2, 1994® abstract: FixL's are chimeric heme protein
kinases from symbiotic nitrogen-fixing Rhizobia. We have overexpressed three FixL variants …

Influence of globin structure on the state of the heme. I. Human deoxyhemoglobin

MF Perutz, JE Ladner, SR Simon, C Ho - Biochemistry, 1974 - ACS Publications
Max F. Perutz,* Jane E. Ladner, Sanford R. Simon, and Chien Ho abstract: Heme-heme
interaction arises through a transition between two alternative quaternary structures of the …

The effect of sulphide on cytochrome aa3. Isosteric and allosteric shifts of the reduced alpha-peak.

P Nicholls - Biochimica et Biophysica Acta, 1975 - europepmc.org
1. Sulphide, like cyanide, is a slow-binding inhibitor of cytochrome aa3 with a high affinity
(KD smaller than 0.1 MUM). 2. Unlike cyanide binding, the binding of sulphide is apparently …

Mechanism of tertiary structural change in hemoglobin.

BR Gelin, M Karplus - … of the National Academy of Sciences, 1977 - National Acad Sciences
A reaction path is presented by which the effects of oxygen binding in hemoglobin are
transmitted from a heme group to the surface of its subunit. Starting from the known deoxy …

Influence of globin structures on the state of the heme. IV. Ferrous low spin derivatives

MF Perutz, JV Kilmartin, K Nagai, A Szabo… - Biochemistry, 1976 - ACS Publications
Studies of high spin ferrous and ferric deriva-tives led us to conclude that in the quaternary R
structure the state of the hemesis similar to that in the free a and ß subunits, but in the T …