Nitric Oxide Synthase: Difference between revisions
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It is also known that H<sub>4</sub>B works as a elctron donor to reduce a oxyferrous complex (HVAD ER DETTE) from Fe (III) to Fe(II), but as stated above, it does not reduce the ferric heme.<ref>PMID: 17014963 </ref> | It is also known that H<sub>4</sub>B works as a elctron donor to reduce a oxyferrous complex (HVAD ER DETTE) from Fe (III) to Fe(II), but as stated above, it does not reduce the ferric heme.<ref>PMID: 17014963 </ref> | ||
It is still not quite certain what the role of H<sub>4</sub>B is. But its structural importense is reconned to play a role in dimer formation, and major conformational changes leading to the formation af the active site channelform.<ref>PMID:9875848</ref>. | It is still not quite certain what the role of H<sub>4</sub>B is. But its structural importense is reconned to play a role in dimer formation, and major conformational changes leading to the formation af the active site channelform.<ref>PMID:9875848</ref>. | ||
The H<sub>4</sub>B is bound by hydrogen-bonds to several of the molekules surrounding it, including the substrate L-Arg. | The H<sub>4</sub>B is bound by hydrogen-bonds to several of the molekules surrounding it, including the substrate L-Arg. The substrate is H-bonded to the 4-keto group of pterin, and to one of the heme propionate groups, that has two carboxylate oxygens in use for H-bonds. These oxygens are further H-bonded to the 4-keto group of pterin, through water, and directly to N(3) and NH<sub>2</sub> on C (2). The big picture of all the H-bonds can be seen on figure (???)-lav figur i chemdraw inspireret af figuren s. 943Raman))) | ||
===Heme=== | ===Heme=== | ||
