Green hemes

Metcalfe CL, Ott M, Patel N et al (2004) Autocatalytic formation of green heme evidence for H202-dependent formation of a covalent methionine-heme linkage in ascorbate peroxidase. J Am Chem Soc 126 16242-16248... 

Green Hemes Iron Chlorins and Iron Formyl-Substituted Porphyrins... 

LA. Andersson, T.M. Loehr, C.K. Chang, and A.G. Mauk, Resonance Raman spectroscopy of metallochlorins models for green heme protein prosthetic groups,/. Am. Chem. Soc. 107 182 (1985). 

R432 M. Nakamura, Nuclear Magnetic Resonance Studies on the Electronic Structure of Green Hemes and Green Heme Proteins , Global J. Inorg. Chem., [online computer file], 2012, 3, 1/1. 

Mo, heme non-heme Fe sulfide Cu (green), heme cd, P450 Heme be non-heme Fe , P-450 Cu (purple)... 

Lian T, Locke B, Kholodenko Y and Hochstrasser R M 1994 Energy flow from solute to solvent probed by femtosecond IR spectroscopy malachite green and heme protein solutions J. Rhys. 

Detecting the presence of small, even invisible, amounts of blood is routine. Physical characteristics of dried stains give minimal information, however, as dried blood can take on many hues. Many of the chemical tests for the presence of blood rely on the catalytic peroxidase activity of heme (56,57). Minute quantities of blood catalyze oxidation reactions between colorless materials, eg, phenolphthalein, luco malachite green, luminol, etc, to colored or luminescent ones. The oxidant is typically hydrogen peroxide or sodium perborate (see Automated instrumentation,hematology). 

Phthalocyanines are analogues of the natural pigments chlorophyll and heme. However, unlike these natural pigments, which have extremely poor stabihty, phthalocyanines are probably the most stable of all the colorants ia use today. Substituents can extend the absorption to longer wavelengths, iato the near iafrared, but not to shorter wavelengths, and so their hues are restricted to blue and green. 

Figure 3.10 Schematic diagram of the glohin domain. The eight a helices are labeled A-H. A-D are red, E and F green, and G and H blue. The heme group is shown in white. (Adapted from orlginais provided by A. Lesk.)...

Figure 12.14 The three-dimensional structure of a photosynthetic reaction center of a purple bacterium was the first high-resolution structure to be obtained from a membrane-bound protein. The molecule contains four subunits L, M, H, and a cytochrome. Subunits L and M bind the photosynthetic pigments, and the cytochrome binds four heme groups. The L (yellow) and the M (red) subunits each have five transmembrane a helices A-E. The H subunit (green) has one such transmembrane helix, AH, and the cytochrome (blue) has none. Approximate membrane boundaries are shown. The photosynthetic pigments and the heme groups appear in black. (Adapted from L. Stryer, Biochemistry, 3rd ed. New York ...

FIGURE 22.18 Model of the R. viridis reaction center, (a, b) Two views of the ribbon diagram of the reaction center. Mand L subunits appear in purple and blue, respectively. Cytochrome subunit is brown H subunit is green. These proteins provide a scaffold upon which the prosthetic groups of the reaction center are situated for effective photosynthedc electron transfer. Panel (c) shows the spatial relationship between the various prosthetic groups (4 hemes, P870, 2 BChl, 2 BPheo, 2 quinones, and the Fe atom) in the same view as in (b), but with protein chains deleted. 

The reddish metal was already known in prehistoric times. It occasionally occurs as a native metal, but mostly in conspicuous green ores, from which it is extracted relatively easily. It is convenient to work, but not very hard. Not very optimal as a tool ("Otzi the Iceman" had a copper axe with him). Only through the addition of tin is the more useful bronze obtained. Its zinc alloy is the versatile and widely used brass. Copper is one of the coinage metals. Water pipes are commonly made of copper. Its very good thermal and electrical conductivity is commonly exploited (cable ), as well as its durability (roofs, gutters), as the verdigris (basic copper carbonate) protects the metal. Cu phthalocyanines are the most beautiful blue pigments. Seems to be essential to all life as a trace element. In some molluscs, Cu replaces Fe in the heme complex. A 70-kg human contains 72 mg. 

Fig. 8. Model for the high affinity complex between horse Cc and CcO determined by Roberts and Pique (34). The backbone of horse Cc and CcO subunit II are shown with the side chains of selected lysines and acidic residues colored blue and red, respectively. The residue numbers on subunit II are for R. sphaeroides CcO. Van der Waals surfaces are shown for Cc heme and subunit II Trp143 and Met263. The CuA coppers are represented by green Corey-Pauling-Koltun models. Reprinted with permission from Ref. (18). Copyright 1999, American Society of Biochemistry and Molecular Biology.

Smithies vertical starch gel electrophoresis (S7) separates the plasma proteins more distinctly than any other method. If the Hp concentration is normal, the Hp type can generally be recognized directly after the staining for proteins, but sensitive and more specific staining for heme groups, e.g., benzidine, o-dianisidine (04), and malachite green (N5) are preferable. This technique consumes more hydrolyzed starch than the simpler original horizontal electrophoresis technique (S5). 

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