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==Overview==

The crystal structures of the oxidized and reduced forms of cytochrome c", from Methylophilus methylotrophus were solved from X-ray synchrotron data, to atomic resolution. The overall fold of the molecule in the two redox, states is very similar and is comparable to that of the oxygen-binding, protein from the purple phototrophic bacterium Rhodobacter sphaeroides., However, significant modifications occur near the haem group, in, particular the detachment from axial binding of His95 observed upon, reduction as well as the adoption of different conformations of some, protonatable residues that form a possible proton path from the haem, pocket to the protein surface. These changes are associated with the, previously well characterized redox-Bohr behaviour of this protein., Furthermore they provide a model for one of the presently proposed, mechanisms of proton translocation in the much more complex protein, cytochrome c oxidase.

The crystal structures of the oxidized and reduced forms of cytochrome c" from Methylophilus methylotrophus were solved from X-ray synchrotron data to atomic resolution. The overall fold of the molecule in the two redox states is very similar and is comparable to that of the oxygen-binding protein from the purple phototrophic bacterium Rhodobacter sphaeroides. However, significant modifications occur near the haem group, in particular the detachment from axial binding of His95 observed upon reduction as well as the adoption of different conformations of some protonatable residues that form a possible proton path from the haem pocket to the protein surface. These changes are associated with the previously well characterized redox-Bohr behaviour of this protein. Furthermore they provide a model for one of the presently proposed mechanisms of proton translocation in the much more complex protein cytochrome c oxidase.

==About this Structure==

Line 13:

[[Category: Methylophilus methylotrophus]]

[[Category: Single protein]]

[[Category: Carrondo, M.A.]]

[[Category: Carrondo, M A.]]

[[Category: Enguita, F.J.]]

[[Category: Enguita, F J.]]

[[Category: Pohl, E.]]

[[Category: Rodrigues, A.]]

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[[Category: oxidoreductase]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-The crystal structures of the oxidized and reduced forms of cytochrome c", from Methylophilus methylotrophus were solved from X-ray synchrotron data, to atomic resolution. The overall fold of the molecule in the two redox, states is very similar and is comparable to that of the oxygen-binding, protein from the purple phototrophic bacterium Rhodobacter sphaeroides., However, significant modifications occur near the haem group, in, particular the detachment from axial binding of His95 observed upon, reduction as well as the adoption of different conformations of some, protonatable residues that form a possible proton path from the haem, pocket to the protein surface. These changes are associated with the, previously well characterized redox-Bohr behaviour of this protein., Furthermore they provide a model for one of the presently proposed, mechanisms of proton translocation in the much more complex protein, cytochrome c oxidase.
+The crystal structures of the oxidized and reduced forms of cytochrome c" from Methylophilus methylotrophus were solved from X-ray synchrotron data to atomic resolution. The overall fold of the molecule in the two redox states is very similar and is comparable to that of the oxygen-binding protein from the purple phototrophic bacterium Rhodobacter sphaeroides. However, significant modifications occur near the haem group, in particular the detachment from axial binding of His95 observed upon reduction as well as the adoption of different conformations of some protonatable residues that form a possible proton path from the haem pocket to the protein surface. These changes are associated with the previously well characterized redox-Bohr behaviour of this protein. Furthermore they provide a model for one of the presently proposed mechanisms of proton translocation in the much more complex protein cytochrome c oxidase.
 ==About this Structure==
@@ Line 13: / Line 13: @@
 [[Category: Methylophilus methylotrophus]]
 [[Category: Single protein]]
-[[Category: Carrondo, M.A.]]
+[[Category: Carrondo, M A.]]
-[[Category: Enguita, F.J.]]
+[[Category: Enguita, F J.]]
 [[Category: Pohl, E.]]
 [[Category: Rodrigues, A.]]
@@ Line 22: / Line 22: @@
 [[Category: oxidoreductase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 09:42:38 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:54:01 2008''