Next Article in Journal
In Silico Evaluation and In Vitro Determination of Neuroprotective and MAO-B Inhibitory Effects of Pyrrole-Based Hydrazones: A Therapeutic Approach to Parkinson’s Disease
Previous Article in Journal
Effect of IL-27, Teriflunomide and Retinoic Acid and Their Combinations on CD4+ T Regulatory T Cells—An In Vitro Study
 
 
Font Type:
Arial Georgia Verdana
Font Size:
Aa Aa Aa
Line Spacing:
Column Width:
Background:
Article

O2 Carrier Myoglobin Also Exhibits β-Lactamase Activity That Is Regulated by the Heme Coordination State

1
School of Chemistry and Chemical Engineering, University of South China, Hengyang 421001, China
2
Lab of Protein Structure and Function, University of South China Medical School, Hengyang 421001, China
3
Department of Chemistry and Institute of Biomedical Science, Fudan University, Shanghai 200433, China
*
Author to whom correspondence should be addressed.
Molecules 2022, 27(23), 8478; https://doi.org/10.3390/molecules27238478
Submission received: 11 November 2022 / Revised: 28 November 2022 / Accepted: 30 November 2022 / Published: 2 December 2022

Abstract

Heme proteins perform a variety of biological functions and also play significant roles in the field of bio-catalysis. The β-lactamase activity of heme proteins has rarely been reported. Herein, we found, for the first time, that myoglobin (Mb), an O2 carrier, also exhibits novel β-lactamase activity by catalyzing the hydrolysis of ampicillin. The catalytic proficiency ((kcat/KM)/kuncat) was determined to be 6.25 × 1010, which is much higher than the proficiency reported for designed metalloenzymes, although it is lower than that of natural β-lactamases. Moreover, we found that this activity could be regulated by an engineered disulfide bond, such as Cys46-Cys61 in F46C/L61C Mb or by the addition of imidazole to directly coordinate to the heme center. These results indicate that the heme active site is responsible for the β-lactamase activity of Mb. Therefore, the study suggests the potential of heme proteins acting as β-lactamases, which broadens the diversity of their catalytic functions.
Keywords: heme protein; myoglobin; β-lactamase; ampicillin; heme coordination heme protein; myoglobin; β-lactamase; ampicillin; heme coordination

Share and Cite

MDPI and ACS Style

Tang, S.; Pan, A.-Q.; Wang, X.-J.; Gao, S.-Q.; Tan, X.-S.; Lin, Y.-W. O2 Carrier Myoglobin Also Exhibits β-Lactamase Activity That Is Regulated by the Heme Coordination State. Molecules 2022, 27, 8478. https://doi.org/10.3390/molecules27238478

AMA Style

Tang S, Pan A-Q, Wang X-J, Gao S-Q, Tan X-S, Lin Y-W. O2 Carrier Myoglobin Also Exhibits β-Lactamase Activity That Is Regulated by the Heme Coordination State. Molecules. 2022; 27(23):8478. https://doi.org/10.3390/molecules27238478

Chicago/Turabian Style

Tang, Shuai, Ai-Qun Pan, Xiao-Juan Wang, Shu-Qin Gao, Xiang-Shi Tan, and Ying-Wu Lin. 2022. "O2 Carrier Myoglobin Also Exhibits β-Lactamase Activity That Is Regulated by the Heme Coordination State" Molecules 27, no. 23: 8478. https://doi.org/10.3390/molecules27238478

APA Style

Tang, S., Pan, A.-Q., Wang, X.-J., Gao, S.-Q., Tan, X.-S., & Lin, Y.-W. (2022). O2 Carrier Myoglobin Also Exhibits β-Lactamase Activity That Is Regulated by the Heme Coordination State. Molecules, 27(23), 8478. https://doi.org/10.3390/molecules27238478

Article Metrics

Back to TopTop