1h57: Difference between revisions

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==Overview==

A molecular description of oxygen and peroxide activation in biological, systems is difficult, because electrons liberated during X-ray data, collection reduce the active centres of redox enzymes catalysing these, reactions. Here we describe an effective strategy to obtain crystal, structures for high-valency redox intermediates and present a, three-dimensional movie of the X-ray-driven catalytic reduction of a bound, dioxygen species in horseradish peroxidase (HRP). We also describe, separate experiments in which high-resolution structures could be obtained, for all five oxidation states of HRP, showing such structures with, preserved redox states for the first time.

A molecular description of oxygen and peroxide activation in biological systems is difficult, because electrons liberated during X-ray data collection reduce the active centres of redox enzymes catalysing these reactions. Here we describe an effective strategy to obtain crystal structures for high-valency redox intermediates and present a three-dimensional movie of the X-ray-driven catalytic reduction of a bound dioxygen species in horseradish peroxidase (HRP). We also describe separate experiments in which high-resolution structures could be obtained for all five oxidation states of HRP, showing such structures with preserved redox states for the first time.

==About this Structure==

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[[Category: Peroxidase]]

[[Category: Single protein]]

[[Category: Berglund, G.I.]]

[[Category: Berglund, G I.]]

[[Category: Carlsson, G.H.]]

[[Category: Carlsson, G H.]]

[[Category: Hajdu, J.]]

[[Category: Henriksen, A.]]

[[Category: Smith, A.T.]]

[[Category: Smith, A T.]]

[[Category: Szoke, H.]]

[[Category: ACT]]

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[[Category: peroxidase]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:57:30 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-A molecular description of oxygen and peroxide activation in biological, systems is difficult, because electrons liberated during X-ray data, collection reduce the active centres of redox enzymes catalysing these, reactions. Here we describe an effective strategy to obtain crystal, structures for high-valency redox intermediates and present a, three-dimensional movie of the X-ray-driven catalytic reduction of a bound, dioxygen species in horseradish peroxidase (HRP). We also describe, separate experiments in which high-resolution structures could be obtained, for all five oxidation states of HRP, showing such structures with, preserved redox states for the first time.
+A molecular description of oxygen and peroxide activation in biological systems is difficult, because electrons liberated during X-ray data collection reduce the active centres of redox enzymes catalysing these reactions. Here we describe an effective strategy to obtain crystal structures for high-valency redox intermediates and present a three-dimensional movie of the X-ray-driven catalytic reduction of a bound dioxygen species in horseradish peroxidase (HRP). We also describe separate experiments in which high-resolution structures could be obtained for all five oxidation states of HRP, showing such structures with preserved redox states for the first time.
 ==About this Structure==
@@ Line 14: / Line 14: @@
 [[Category: Peroxidase]]
 [[Category: Single protein]]
-[[Category: Berglund, G.I.]]
+[[Category: Berglund, G I.]]
-[[Category: Carlsson, G.H.]]
+[[Category: Carlsson, G H.]]
 [[Category: Hajdu, J.]]
 [[Category: Henriksen, A.]]
-[[Category: Smith, A.T.]]
+[[Category: Smith, A T.]]
 [[Category: Szoke, H.]]
 [[Category: ACT]]
@@ Line 32: / Line 32: @@
 [[Category: peroxidase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 09:46:32 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:57:30 2008''