Porphyrin-substituted H-NOX proteins as high-relaxivity MRI contrast agents.

ABSTRACT: Heme proteins are exquisitely tuned to carry out diverse biological functions while employing identical heme cofactors. Although heme protein properties are often altered through modification of the protein scaffold, protein function can be greatly expanded and diversified through replacement of the native heme with an unnatural porphyrin of interest. Thus, porphyrin substitution in proteins affords new opportunities to rationally tailor heme protein chemical properties for new biological applications. Here, a highly thermally stable Heme Nitric oxide/OXygen binding (H-NOX) protein is evaluated as a magnetic resonance imaging (MRI) contrast agent. T1 and T2 relaxivities measured for the H-NOX protein containing its native heme are compared to the protein substituted with unnatural manganes

SUBMITTER: Winter MB 

PROVIDER: S-EPMC3594055 | biostudies-literature | 2013 Mar

REPOSITORIES: biostudies-literature