Biochemistry of Hemoglobin

Carbon 2 in glycerate-2,3-bisphosphate is in the D configuration. Would you expect the l configuration of glycerate-2,3-bisphosphate to have the same effect on the biochemistry of hemoglobin Why or why not ... 

Biomimetic detectors Another relatively simple device for detecting CO utilizes the reversible reaction of CO with an iron(II) compound held in a porous matrix to produce a color change that can be measured optically. The iron compound may be a synthetic porphyrin, which in a sense mimics the biochemistry of hemoglobin hence these detectors are... 

Orttung, WH, Proton Binding and Dipole Moment of Hemoglobin. Refined Calculations, Biochemistry 9, 2394, 1970. 

Y. Nomura and M. Tamura. Quantitative analysis of hemoglobin oxygenation state of rat brain in vivo by picosecond time-resolved spectrophotometry. Journal of Biochemistry, 109 455-461, 1991. 

Szebeni J, Hauser H, Eskelson CD, et al. Interaction of hemoglobin derivatives with liposomes. Membrane cholesterol protects against the changes of hemoglobin. Biochemistry 1988 27 6425. 

Andreyuk GM, Kisel MA. Conversion of hemoglobin to hemichrome by lysophospholipids. Biochemistry (Mosc) 64, 867, 1999. 

Szebeni J, Di lorio EE, Hauser H, et al. Encapsulation of hemoglobin in phospholipid liposomes characterization and stability. Biochemistry 1985 24 2827. 

Nagai, M., et al. (1991) Unusual CO bonding geometry in abnormal subunits of hemoglobin M Boston hemoglobin M Saskatoon. Biochemistry 30, 6495-6503. 

Sharma, V. S., Traylor, T. G., Gardiner, R., and Mizukami, H. (1987). Reaction of nitric oxide with heme proteins and model compounds of hemoglobin. Biochemistry 26, 3837-3843. 

TThe iron-porphyrin (heme) group of hemoglobin, released from dying erythrocytes in the spleen, is degraded to yield free Fes+ and, ultimately, bilirubin. This pathway is arresting for its capacity to inject color into human biochemistry. 

Myoglobin is a heme protein found in the skeletal muscle of meat-producing animals. It provides the red color associated with meat and thus affects the appearance of meat. Two other heme-containing proteins found in meat are hemoglobin and cytochromes. These are generally present at relatively low concentrations and are not considered to substantially impact the color of meat from normal animals (Warriss and Rhodes, 1977 Ledward, 1984). Several reviews have been published on the biochemistry of myoglobin and its relevance in meat (Faustman and Cassens, 1990 Renerre, 1990 Cornforth, 1994). 

Dickerson, R. E., and I. Geis, Hemoglobin. Menlo Park, Calif. Benjamin/Cummings, 1983. A magnificent presentation of every facet of hemoglobin biochemistry and genetics. 

Gladwin, M.T., Crawford, J.H., and Ratel, R.R. 2004. The biochemistry of nitric oxide, nitrite and hemoglobin Role in blood flow regulation. Free Radical Biology Medicine, 36 707-17. 

Huang Y, Ackers GK. Transformation of cooperative free energies between ligation systems of hemoglobin resolution of the carbon monoxide binding intermediates. Biochemistry 1996 35 704-718. 

Ackers GK, Holt JM. Asymmetric cooperativity in a symmetric tetramer human hemoglobin. J. Biol. Chem. 2006 281 11441-11443. Jayaraman V, Spiro TG. Structure of a third cooperativity state of hemoglobin ultraviolet resonance Raman spectroscopy of cyanome-themoglobin ligation microstates. Biochemistry 1995 34 4511 515. 

Whereas compartmental models are abstract mathematical representations of an animal or a human body, in the form of a certain number of boxes, PBPK models describe the behavior of xenobiotics on the basis of the actual anatomy, physiology, and biochemistry of human beings and animals. Being realistically modeled on how the body functions, PBPK models take into consideration the complex relationships that exist between critical biological and physicochemical determinants such as blood flow, ventilation rates, metabolic rate constants, tissue solubilities, and binding to proteins (e.g., albumin and glycoproteins) or other macromolecules (e.g., DNA and hemoglobin). 

Benesch RE, Benesch R, Yu CL The oxygenation of hemoglobin in the presence of 2,3-diphosphoglycer-ate. Effect of temperature, pH, ionic strength, and hemoglobin concentration. Biochemistry 1969 8 2567-71. 

Hazard Dust and fine particles suspended in air are flammable and an explosion risk. TLV (as oxide fume) 5 mg/m3 for soluble salts (as iron) 1 mg/m3. Biochemistry Iron is a constituent of hemoglobin and is essential to plant and animal life, an important factor in cellular oxidation mechanism. 

M. F. Perutz Regulation of oxygen affinity of hemoglobin Influence of structure of the globin on the heme iron. Annual Review of Biochemistry 48,327(1979). 

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