Calcium complexes binding

In addition to phosphorylase b kinase, the calmodulin-calcium complex binds to other proteins, including the myosin light chain kinase in muscle, which helps to stimulate muscular contraction. 

Calcium-binding proteins, 6, 564, 572, 596 intestinal, 6, 576 structure, 6, 573 Calcium carbonate calcium deposition as, 6, 597 Calcium complexes acetylacetone, 2, 372 amides, 2,164 amino acids, 3, 33 arsine oxides, 3, 9 biology, 6, 549 bipyridyl, 3, 13 crown ethers, 3, 39 dimethylphthalate, 3, 16 enzyme stabilization, 6, 549 hydrates, 3, 7 ionophores, 3, 66 malonic acid, 2, 444 peptides, 3, 33 phosphines, 3, 9 phthalocyanines, 2,863 porphyrins, 2, 820 proteins, 2, 770 pyridine oxide, 3,9 Schiff bases, 3, 29 urea, 3, 9... 

Platelet membrane phosphatidylserine is critical to the formation of the tenase complex since on its surface activated factor VIII (Villa) generates a high-afflnity binding site for activated factor IX (IXa) in the presence of calcium. Subsequently, this complex activates factor X (2, 13). Platelet membrane phosphatidylserine similarly anchors activated factor V (Va), favoring the calcium-dependent binding of activated factor X (Xa). The prothrombinase complex is generated on the surface of the anionic platelet membrane phosphatidylserine when factor Va binds prothrombin. The prothrombinase complex cleaves prothrombin to produce thrombin, which has a multifunctional role (14). 

Schematic illustration of the conversion of L-arginine to NO plus L-citrulline by the enzyme NO synthase. Conversion requires the presence of NADPH, calcium (Ca), calmodulin (CM), and O2. Calcium complexes with CM and the Ca-CM complex binds to the enzyme. The asterisk signifies the basic amino nitrogen atom that undergoes oxidation and cleavage to form NO. Both of the basic amino nittogens are equivalent and either nitrogen can be incorporated into NO.

Coordination chemistry of RE(III) with amino acids has been attracting much interest since the early 1970s after the discovery that certain RE(III) ions could be used as probes of calcium ion binding sites in proteins and enzymes [118, 119], Since then, a large amount of work on the solution and structural chemistry of rare earth-amino acid complexes has been published. The solution studies involve all of the rare earth elements and 13 (Gly, Ala, Val, Leu, Phe, Met, Pro, Ser, Tyr, His, Lys, Trp, and Arg) of the 20 standard amino acids, and more than 100 of the RE(III)-amino acid complexes have been structurally characterized. This section will cover the synthetic, structural, and solution chemistry of these complexes. 

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