Corrole-Substituted Fluorescent Heme Proteins.

Corrole-Substituted Fluorescent Heme Proteins.
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DOI:
10.1021/acs.inorgchem.0c03599
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发表时间:
2021-02-15
影响因子:
4.6
通讯作者:
Marletta MA
Marletta MA
中科院分区:
化学2区
文献类型:
--
作者:
Lemon CM;Marletta MA

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Although fluorescent proteins have been utilized for a variety of biological applications, they have several optical limitations, namely weak red and NIR emission and exceptionally broad (> 200 nm) emission profiles. The photophysical properties of fluorescent proteins can be enhanced through the incorporation of novel cofactors with the desired properties into a stable protein scaffold. To this end, a fluorescent phosphorus corrole that is structurally similar to the native heme cofactor is incorporated into two exceptionally stable heme proteins: H-NOX from Caldanaerobacter subterraneus and HasA from Pseudomonas aeruginosa. These yellow-orange emitting protein conjugates are examined by steady-state and time-resolved optical spectroscopy. The HasA conjugate exhibits enhanced fluorescence, whereas emission from the H-NOX conjugate is quenched relative to the free corrole. Despite the low fluorescence quantum yields, these corrole-substituted proteins exhibit more intense fluorescence in a narrower spectral profile than traditional fluorescent proteins that emit in the same spectral window. This study demonstrates that fluorescent corrole complexes are readily incorporated into heme proteins and provides an inroad for the development of novel fluorescent proteins.
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