AI Article Synopsis

  • Proteolytic digestion of nitrite reductase from Pseudomonas aeruginosa leads to the isolation of a d1 heme domain made up of two peptides that are noncovalently linked.
  • This d1 domain can consume oxygen and binds carbon monoxide slightly better than the full dimeric form of the enzyme.
  • However, it loses the ability to oxidize cytochrome c551, indicating that the two domains do not strongly interact and are merely parts of the same polypeptide.

Article Abstract

Proteolitic digestion of nitrite reductase from Pseudomonas aeruginosa allows to obtain and purify a domain containing only the d1 heme and constituted by two noncovalently bound peptides. This d1 domain catayzes oxygen consumption, and binds carbon monoxide with a kinetic constant slightly higher than the parental dimeric holoenzyme. The capacity to oxidize the physiological substrate, cytochrome c551, is lost, even when the proteolytic c heme domain is added to this reaction mixture. This finding suggests that the two domains do not have a significant affinity for each other, and are kept together only by being part of the same polypeptide.

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http://dx.doi.org/10.1016/0162-0134(95)00090-9DOI Listing

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