Direct Measurements of the Cobalt‐Thiolate Bonds Strength in Rubredoxin by Single‐Molecule Force Spectroscopy

Shi, Shuting; Wu, Tao; Zheng, Peng

doi:10.1002/cbic.202200165

Cited by 3 publications

(2 citation statements)

References 74 publications

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“…The pathway to rupture the iron-thiolate bonds is bifurcated and may lead to unfolding intermediate states with a partially ruptured iron–sulfur center ,,, (Figure A). In addition, owing to the similar mechanical strength of other metal thiolate bonds, metalloproteins containing a non-iron metal sulfur center, such as zinc and cobalt rubredoxin, , metallothionein , (which binds multiple Zn 2+ ), and DnaJ Hsp40 chaperone (which contains two ZnS4 centers), were shown to follow a similar mechanical unfolding pathway.…”

Section: Smfs Studies Revealed a General Mechanical Unfolding Pathway...mentioning

confidence: 99%

Single Molecule Force Spectroscopy Studies on Metalloproteins: Opportunities and Challenges

2023

Langmuir

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Metalloproteins play important roles in a wide range of biological processes. Elucidating the mechanisms via which metalloproteins fold and constitute their metal centers is critical to the understanding of the functions and dynamics of metalloproteins. Owing to its superior force and length resolution, single-molecule force spectroscopy (SMFS) has evolved into a powerful tool to probe the unfolding and folding mechanisms of metalloproteins at the single level by forcing metalloproteins to unfold and then refold along a reaction coordinate defined by the applied stretching force. The folding of metalloproteins is complex and involves two interwound processes, the folding of the polypeptide chain and the constitution of the metal center. Experimental studies of the folding of metalloproteins are challenging. SMFS studies have allowed researchers to directly probe the folding and unfolding of metalloproteins at the single-molecule level and the effect of metal centers on the folding−unfolding energy landscape of metalloproteins. New mechanistic insights on the folding and unfolding of some metalloproteins have been obtained, demonstrating the power and unique advantages that SMFS techniques may offer. In this Perspective, using calcium-binding proteins and small iron−sulfur proteins as examples, I provide a concise overview of the information and insights that SMFS studies have provided to understand the folding and unfolding of metalloproteins. I also discuss the opportunities and challenges that are present in this fast-progressing area of research.

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Section: Smfs Studies Revealed a General Mechanical Unfolding Pathway...mentioning

confidence: 99%

Single Molecule Force Spectroscopy Studies on Metalloproteins: Opportunities and Challenges

2023

Langmuir

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“…In addition to visualization and obtaining mechanical properties, it is possible to record the physicochemical properties of samples via the AFM method when modifying the equipment. For example, using AFM-based force spectroscopy (AFM-FS), which makes it possible to study the forces of biomolecular adhesion at the level of individual molecules [11], one can obtain information about the intramolecular interactions of proteins and DNA/RNA chains [12] as well as analyze the molecular interactions of two single biomolecules attached to the substrate surface and AFM tip [13]. There are data on the implementation of the wavelet cross-correlation (XWT) technique in atomic force spectroscopy with simultaneous excitation of high cantilever modes to reproduce complex force dynamics with probe-sample contact [14].…”

Section: Introductionmentioning

confidence: 99%

Analytical Models for Measuring the Mechanical Properties of Yeast

Savin

Erofeev

Gorelkin

2023

Cells

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The mechanical properties of yeast play an important role in many biological processes, such as cell division and growth, maintenance of internal pressure, and biofilm formation. In addition, the mechanical properties of cells can indicate the degree of damage caused by antifungal drugs, as the mechanical parameters of healthy and damaged cells are different. Over the past decades, atomic force microscopy (AFM) and micromanipulation have become the most widely used methods for evaluating the mechanical characteristics of microorganisms. In this case, the reliability of such an estimate depends on the choice of mathematical model. This review presents various analytical models developed in recent years for studying the mechanical properties of both cells and their individual structures. The main provisions of the applied approaches are described along with their limitations and advantages. Attention is paid to the innovative method of low-invasive nanomechanical mapping with scanning ion-conductance microscopy (SICM), which is currently starting to be successfully used in the discovery of novel drugs acting on the yeast cell wall and plasma membrane.

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Intramolecular Covalent Bonds in Gram‐Positive Bacterial Surface Proteins

Lei

Cao

2022

ChemBioChem

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Gram-positive bacteria experience considerable mechanical perturbation when adhering to host surfaces during colonization and infection. They have evolved various adhesion proteins that are mechanically robust to ensure strong surface adhesion. Recently, it was discovered that these adhesion proteins contain rare, extra intramolecular covalent bonds that stabilize protein structures and participate in surface bonding. These intramolecular covalent bonds include isopeptides, thioesters, and ester bonds, which often form spontaneously without the need for additional enzymes. With the development of singlemolecule force spectroscopy techniques, the detailed mechanical roles of these intramolecular covalent bonds have been revealed. In this review, we summarize the recent advances in this area of research, focusing on the link between the mechanical stability and function of these covalent bonds in Gram-positive bacterial surface proteins. We also highlight the potential impact of these discoveries on the development of novel antibiotics and chemical biology tools.

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Direct Measurements of the Cobalt‐Thiolate Bonds Strength in Rubredoxin by Single‐Molecule Force Spectroscopy

Cited by 3 publications

References 74 publications

Single Molecule Force Spectroscopy Studies on Metalloproteins: Opportunities and Challenges

Single Molecule Force Spectroscopy Studies on Metalloproteins: Opportunities and Challenges

Analytical Models for Measuring the Mechanical Properties of Yeast

Intramolecular Covalent Bonds in Gram‐Positive Bacterial Surface Proteins

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