The Role of Mass Spectrometry in Structural Studies of Flavin-Based Electron Bifurcating Enzymes

Frontiers in Microbiology
Monika Tokmina-LukaszewskaBrian Bothner

Abstract

For decades, biologists and biochemists have taken advantage of atomic resolution structural models of proteins from X-ray crystallography, nuclear magnetic resonance spectroscopy, and more recently cryo-electron microscopy. However, not all proteins relent to structural analyses using these approaches, and as the depth of knowledge increases, additional data elucidating a mechanistic understanding of protein function is desired. Flavin-based electron bifurcating enzymes, which are responsible for producing high energy compounds through the simultaneous endergonic and exergonic reduction of two intercellular electron carriers (i.e., NAD+ and ferredoxin) are one class of proteins that have challenged structural biologists and in which there is great interest to understand the mechanism behind electron gating. A limited number of X-ray crystallography projects have been successful; however, it is clear that to understand how these enzymes function, techniques that can reveal detailed in solution information about protein structure, dynamics, and interactions involved in the bifurcating reaction are needed. In this review, we cover a general set of mass spectrometry-based techniques that, combined with protein modeling, are capabl...Continue Reading

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Citations

Aug 14, 2019·Mass Spectrometry Reviews·Fabio P Gomes, John R Yates
Jul 9, 2020·Computational and Structural Biotechnology Journal·Seungjin Na, Eunok Paek

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Methods Mentioned

BETA
X-ray
nuclear magnetic resonance
protein folding
footprinting
protein exchange
NMR

Software Mentioned

IMS
NMS
SL
XL
ClusPro2
RaptorX
TASSER
PeptideShaker
SearchGUI
SwissDock

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