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Munirathinam Sundaramoorthy

Bio: Munirathinam Sundaramoorthy is an academic researcher from Vanderbilt University. The author has contributed to research in topics: Peroxidase & Cytochrome c peroxidase. The author has an hindex of 23, co-authored 30 publications receiving 2897 citations. Previous affiliations of Munirathinam Sundaramoorthy include University of California, Irvine & University of Kansas.

Papers
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TL;DR: In this article, the authors have shown that mutations in genes corresponding to the building blocks of type IV collagen cause Alport's syndrome, whereas autoantibodies against structures that are usually hidden in the recesses of collagen IV cause Goodpasture's syndrome.
Abstract: Defects in type IV collagen, a collagenous protein involved in the formation of basement membranes, have been implicated in hereditary Alport's syndrome and acquired Goodpasture's syndrome. Mutations in genes corresponding to the building blocks of type IV collagen cause Alport's syndrome, whereas autoantibodies against structures that are usually hidden in the recesses of collagen IV cause Goodpasture's syndrome.

843 citations

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TL;DR: The structure determination of CPO was undertaken to help elucidate those structural features that enable the enzyme to exhibit these multiple activities of peroxidase, catalase and cytochrome P450-like activities in addition to catalyzing halogenation reactions.

384 citations

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TL;DR: The crystal structure of manganese peroxidase (MnP) from the lignin-degrading basidiomycetous fungus Phanerochaete chrysosporium has been solved using molecular replacement techniques and a new cation binding site was located in the crystal structure.

373 citations

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TL;DR: In this article, the structural basis for peptide and network assembly was investigated by determining the crystal structure of the ubiquitous ((alpha1)(2).alpha2]-hexamer of bovine lens capsule basement membrane at 2.0 A resolution.

159 citations

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TL;DR: Molecular modeling and dynamics simulations of CPO with the substrate cis-beta methylstyrene and the corresponding epoxide products provide a structural and energetic basis for understanding the enantioselectivity of C PO-catalyzed epoxidation reactions.

152 citations


Cited by
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Journal ArticleDOI
TL;DR: Proton-coupled electron transfer is an important mechanism for charge transfer in a wide variety of systems including biology- and materials-oriented venues and several are reviewed.
Abstract: ▪ Abstract Proton-coupled electron transfer (PCET) is an important mechanism for charge transfer in a wide variety of systems including biology- and materials-oriented venues. We review several are...

2,182 citations

Journal ArticleDOI
TL;DR: This review will concentrate on findings with P-450cam of the Pseudomonas putida camphor-5-exo-hydroxylase, and attention will be drawn to parallel and contrasting examples from other P- 450s as appropriate.
Abstract: Two decades have passed since the discovery in liver microsomes of a haemprotein that forms a reduced-CO complex with the absorptive maximum of the Soret at 450 nm (Klingenberg, 1958; Garfinkel, 1958) and the identification of this protein as a new cytochrome: pigment cytochrome, P-450 (Omura and Sato, 1962, 1964a). In the intervening years, the study of cytochrome P-450 dependent monoxygenases has expanded exponentially. From the first crude attempts to solubilise a P-450 (Omura and Sato, 1963, 1964b) to the determination of the primary, secondary, and tertiary structure of cytochrome P-450cam by amino acid sequencing (Haniu et al., 1982a,b) and x-ray crystallography (Poulos et al., 1984) our understanding of this unique family of proteins has been advancing on all fronts. Since, perhaps, the greatest understanding of the structure and mechanism of P-450s has come from concentrated study of P-450cam of the Pseudomonas putida camphor-5-exo-hydroxylase, this review will concentrate on findings with P-450cam; attention will be drawn to parallel and contrasting examples from other P-450s as appropriate.

1,721 citations

Journal ArticleDOI
TL;DR: The basement membrane (BM) as mentioned in this paper is a specialized form of extracellular matrix (ECM) which mediates tissue compartmentalization and sends signals to epithelial cells about the external microenvironment.
Abstract: In recent years, the basement membrane (BM)--a specialized form of extracellular matrix (ECM)--has been recognized as an important regulator of cell behaviour, rather than just a structural feature of tissues. The BM mediates tissue compartmentalization and sends signals to epithelial cells about the external microenvironment. The BM is also an important structural and functional component of blood vessels, constituting an extracellular microenvironment sensor for endothelial cells and pericytes. Vascular BM components have recently been found to be involved in the regulation of tumour angiogenesis, making them attractive candidate targets for potential cancer therapies.

1,560 citations