Design of silk proteins with increased heme binding capacity and fabrication of silk-heme materials.

Abstract:

:In our previous studies, heme was bound into honeybee silk to generate materials that could function as nitric oxide sensors or as recoverable heterogeneous biocatalysts. In this study, we sought to increase the heme-binding capacity of the silk protein by firstly redesigning the heme binding site to contain histidine as the coordinating residue and secondly, by adding multiple histidine residues within the core of the coiled coil core region of the modified silk protein. We used detergent and a protein denaturant to confirm the importance of the helical structure of the silk for heme coordination. Aqueous methanol treatment, which was used to stabilize the materials, transformed the low-spin, six-coordinate heme to a five-coordinate high-spin complex, thus providing a vacant site for ligand binding. The optimal aqueous methanol treatment time that simultaneously maintains the helical protein structure and stabilizes the silk material without substantial leaching of heme from the system was determined.

journal_name

J Inorg Biochem

authors

Rapson TD,Liu JW,Sriskantha A,Musameh M,Dunn CJ,Church JS,Woodhead A,Warden AC,Riley MJ,Harmer JR,Noble CJ,Sutherland TD

doi

10.1016/j.jinorgbio.2017.08.031

subject

Has Abstract

pub_date

2017-12-01 00:00:00

pages

219-227

eissn

0162-0134

issn

1873-3344

pii

S0162-0134(17)30290-8

journal_volume

177

pub_type

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