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ABSTRACT: Blue copper oxidase (BCO) is a multicopper oxidase (MCO) found in Nitrosomonas europaea as well as in other ammonia-oxidizing organisms. In this chapter, we detail methods used to detect, isolate, and characterize BCO from N. europaea. A method for identifying and classifying MCOs commonly found in nitrifiers based on primary sequence is also described.
Methods in enzymology 01/2011; 496:423-33. · 1.90 Impact Factor
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09/2010; , ISBN: 9780470028636
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ABSTRACT: The two-domain multicopper oxidases are proposed to be key intermediates in the evolution of three-domain multicopper oxidases.
A number of two-domain multicopper oxidases have been identified from genome sequences and are classified as type A, type
B, or type C on the basis of the predicted location of the type 1 copper center. The crystal structure of blue copper oxidase,
a type C two-domain multicopper oxidase from Nitrosomonas europaea, has been determined to 1.9 Å resolution. Blue copper oxidase is a trimer, of which each subunit comprises two cupredoxin
domains. Each subunit houses a type 1 copper site in domain 1 and a type 2/type 3 trinuclear copper cluster at the subunit-subunit
interface. The coordination geometry at the trinuclear copper site is consistent with reduction of the copper ions. Although
the overall architecture of blue copper oxidase is similar to nitrite reductases, detailed structural alignments show that
the fold and domain orientation more closely resemble the three-domain multicopper oxidases. These observations have important
implications for the evolution of nitrite reductases and multicopper oxidases.
Journal of Biological Chemistry 04/2009; 284(15):10174-10180. · 4.77 Impact Factor
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ABSTRACT: The two-domain multicopper oxidases are proposed to be key intermediates in the evolution of three-domain multicopper oxidases. A number of two-domain multicopper oxidases have been identified from genome sequences and are classified as type A, type B, or type C on the basis of the predicted location of the type 1 copper center. The crystal structure of blue copper oxidase, a type C two-domain multicopper oxidase from Nitrosomonas europaea, has been determined to 1.9 A resolution. Blue copper oxidase is a trimer, of which each subunit comprises two cupredoxin domains. Each subunit houses a type 1 copper site in domain 1 and a type 2/type 3 trinuclear copper cluster at the subunit-subunit interface. The coordination geometry at the trinuclear copper site is consistent with reduction of the copper ions. Although the overall architecture of blue copper oxidase is similar to nitrite reductases, detailed structural alignments show that the fold and domain orientation more closely resemble the three-domain multicopper oxidases. These observations have important implications for the evolution of nitrite reductases and multicopper oxidases.
Journal of Biological Chemistry 03/2009; 284(15):10174-80. · 4.77 Impact Factor
