Methods to Unravel the Roles of ATPases in Fe-S Cluster Biosynthesis

Molé, Christa N; Dave, Kinjal; Perlstein, Deborah L.

doi:10.1007/978-1-0716-1605-5_9

Cited by 1 publication

(1 citation statement)

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“… 62 Recently, Perlstein and co-workers have provided a biochemical roadmap for exploring the roles of ATP-binding sites and ATPase activity for proteins involved in Fe–S cluster biogenesis. 71 …”

Section: Fe–s Cluster Biogenesis Utilizes Atpasesmentioning

confidence: 99%

The role of nucleoside triphosphate hydrolase metallochaperones in making metalloenzymes

Vaccaro

Drennan

2022

Metallomics

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Metalloenzymes catalyze a diverse set of challenging chemical reactions that are essential for life. These metalloenzymes rely on a wide range of metallocofactors, from single metal ions to complicated metallic clusters. Incorporation of metal ions and metallocofactors into apo-proteins often requires the assistance of proteins known as metallochaperones. Nucleoside triphosphate hydrolases (NTPases) are one important class of metallochaperones and are found widely distributed throughout the domains of life. These proteins use the binding and hydrolysis of nucleoside triphosphates, either adenosine triphosphate (ATP) or guanosine triphosphate (GTP), to carry out highly specific and regulated roles in the process of metalloenzyme maturation. Here, we review recent literature on NTPase metallochaperones and describe the current mechanistic proposals and available structural data. By using representative examples from each type of NTPase, we also illustrate the challenges in studying these complicated systems. We highlight open questions in the field and suggest future directions. This minireview is part of a special collection of articles in memory of Professor Deborah Zamble, a leader in the field of nickel biochemistry.

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Section: Fe–s Cluster Biogenesis Utilizes Atpasesmentioning

confidence: 99%