Salt bridges govern the structural heterogeneity of heme protein interactions and porphyrin networks: microperoxidase-11.

ABSTRACT: In this work, a proteolytic digest of cytochrome c (microperoxidase 11, MP-11) was used as a model to study the structural aspects of heme protein interactions and porphyrin networks. The MP-11 structural heterogeneity was studied as a function of the starting pH (e.g., pH 3.1-6.1) and concentration (e.g., 1-50 μM) conditions and adduct coordination. Trapped ion mobility spectrometry coupled to mass spectrometry (TIMS-MS) showed the MP-11 structural dependence of the charge state distribution and molecular ion forms with the starting pH conditions. The singly charged (e.g., [M]⁺, [M - 2H + NH₄]⁺, [M - H + Na]⁺ and [M - H + K]⁺) and doubly charged (e.g., [M + H]²⁺, [M - H + NH₄]^2+</

SUBMITTER: Porter J 

PROVIDER: S-EPMC9056719 | biostudies-literature | 2020 Sep

REPOSITORIES: biostudies-literature