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putidaredoxin

 
National Institutes of Health

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Highly Cited
2013
Highly Cited
2013
Cytochrome P450cam catalyzes the hydroxylation of camphor in a complex process involving two electron transfers (ETs) from the… Expand
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Highly Cited
2007
Highly Cited
2007
X-ray damage to protein crystals is often assessed on the basis of the degradation of diffraction intensity, yet this measure is… Expand
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Highly Cited
1996
Highly Cited
1996
Putidaredoxin (Pdx) is a Fe2S2 ferredoxin which acts as the physiological reductant of cytochrome P-450cam (CYP101). A model for… Expand
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Highly Cited
1990
Highly Cited
1990
The oxidation of camphor by cytochrome P-450cam requires the participation of a flavoprotein, putidaredoxin reductase, and an… Expand
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Highly Cited
1989
Highly Cited
1989
Cytochrome b5 has been genetically engineered to afford a fluorescent derivative capable of monitoring its association with… Expand
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Highly Cited
1989
Highly Cited
1989
Site-directed mutants of cytochrome P-450cam (the cytochrome P-450 that acts as the terminal monooxygenase in the d-camphor… Expand
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Highly Cited
1988
Highly Cited
1988
A study of the single turnover kinetics of the reaction between oxycytochrome P-450cam and reduced putidaredoxin was performed… Expand
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Highly Cited
1978
Highly Cited
1978
Publisher Summary This chapter discusses the components of bacterial P-450 cam methylene monooxygenase. Hydroxylation by a… Expand
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Highly Cited
1976
Highly Cited
1976
Oxy-ferrous substrate-bound cytochrome P-450cam (mrsO2) autooxidizes in the absence of its specific effector protein… Expand
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Highly Cited
1974
Highly Cited
1974
Methylene hydroxylation by cytochrome P-450(cam) (cytochrome m) can be resolved into four distinct steps: substrate addition, m(o… Expand
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