1H nuclear magnetic resonance study of the prosthetic group in sulfhemoglobin

Chatfield, Mariann J.; Mar, Gerd N. La

doi:10.1016/0003-9861(92)90520-7

Cited by 17 publications

(19 citation statements)

References 29 publications

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“…Ferric sulfcatalase was also observed with absorption bands at 585 nm and 710 nm. Based on this, Bersofsky suggested that the structure of sulfcatalase should be similar to sulfMb and sulfHb [26, 44, 47, 69]. Therefore, these observations support the notion that the sulfheme product is generated in presence of O 2 and/or H 2 O 2 and that the distal His residue near the iron regulates sulfheme formation.…”

Section: Interaction Of H2s With Enzymesmentioning

confidence: 59%

“…Based on the optical spectra reported by Nakamura it is plausible that the MMI radical interacts with the heme and generates sulflactoperoxidase, which inhibit the enzyme activity[43]. A similar mechanism can be invoked for the inactivation of LPO by H 2 S. Moreover, the fact that the optical spectra of LPO in the presence of H 2 S and H 2 O 2 shows bands similar to sulfHb and sulfMb, strongly suggest that the heme group of the sulflactoperoxidase derivative is a chlorin type structure in which the sulfur atom is incorporated across the β-β double bond of the pyrrole B [44, 47, 69]. …”

Section: Interaction Of H2s With Enzymesmentioning

confidence: 99%

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Hydrogen sulfide activation in hemeproteins: The sulfheme scenario

Ríos-González¹,

Román-Morales²,

Pietri³

et al. 2014

Journal of Inorganic Biochemistry

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Traditionally known as a toxic gas, hydrogen sulfide (H2S) is now recognized as an important biological molecule involved in numerous physiological functions. Like nitric oxide (•NO) and carbon monoxide (CO), H2S is produced endogenously in tissues and cells and can modulate biological processes by acting on target proteins. For example, interaction of H2S with the oxygenated form of human hemoglobin and myoglobin produces a sulfheme protein complex that has been implicated in H2S degradation. The presence of this sulfheme derivative has also been used as a marker for endogenous H2S synthesis and metabolism. Remarkably, human catalases and peroxidases also generate this sulfheme product. In this review, we describe the structural and functional aspects of the sulfheme derivative in these proteins and postulate a generalized mechanism for sulfheme protein formation. We also evaluate the possible physiological function of this complex and highlight the issues that remain to be assessed to determine the role of sulheme proteins in H2S metabolism, detection and physiology.

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Section: Interaction Of H2s With Enzymesmentioning

confidence: 59%

Section: Interaction Of H2s With Enzymesmentioning

confidence: 99%

Hydrogen sulfide activation in hemeproteins: The sulfheme scenario

Ríos-González¹,

Román-Morales²,

Pietri³

et al. 2014

Journal of Inorganic Biochemistry

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“…In Mb and Hb, H 2 S can also bind and modify the heme. The resulting derivatives, named sulfmyoglobin, sulfhemoglobin, or sulfheme species (6)(7)(8)(9)16), have lower O 2 affinity, thereby reducing O 2 transport and ATP production in the mitochondria, which can in principle, also activate the K ATP channels.…”

Section: Introductionmentioning

confidence: 99%

“…It was later shown that these sulfhemoglobin and sulfmyoglobin complexes consisted of a chlorin type heme in which one of the pyrrole rings was modified by the incorporation of the sulfur atom across the b-b double bond of the pyrrole ''B'' (Fig. 4) (6)(7)(8)(9)16). Incorporation of the sulfur atom was suggested to remove electron density from the ferrous iron toward the periphery of the chlorin ring.…”

mentioning

confidence: 99%

Hydrogen Sulfide and Hemeproteins: Knowledge and Mysteries

Pietri

Román-Morales

López‐Garriga

2011

Antioxidants & Redox Signaling

190

136

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Historically, hydrogen sulfide (H(2)S) has been regarded as a poisonous gas, with a wide spectrum of toxic effects. However, like ·NO and CO, H(2)S is now referred to as a signaling gas involved in numerous physiological processes. The list of reports highlighting the physiological effects of H(2)S is rapidly expanding and several drug candidates are now being developed. As with ·NO and CO, not a single H(2)S target responsible for all the biological effects has been found till now. Nevertheless, it has been suggested that H(2)S can bind to hemeproteins, inducing different responses that can mediate its effects. For instance, the interaction of H(2)S with cytochrome c oxidase has been associated with the activation of the ATP-sensitive potassium channels, regulating muscle relaxation. Inhibition of cytochrome c oxidase by H(2)S has also been related to inducing a hibernation-like state. Although H(2)S might induce these effects by interacting with hemeproteins, the mechanisms underlying these interactions are obscure. Therefore, in this review we discuss the current state of knowledge about the interaction of H(2)S with vertebrate and invertebrate hemeproteins and postulate a generalized mechanism. Our goal is to stimulate further research aimed at evaluating plausible mechanisms that explain H(2)S reactivity with hemeproteins.

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“…The spectroscopic alterations which occur only in the presence of oxygen, accompany the irreversible formation of a new hemoglobin derivative, sulfhemoglobin [1,34,35]. The green Hb derivative results from a covalent modification by sulfide of one of the pyrrole rings of the heme [36][37][38][39]. Reduced sulfhemoglobin has a higher oxygen affinity and lower cooperativity than normal human Hb and is practically non-functional in O 2 transport [37].…”

Section: Sulfide and Hemoglobinmentioning

confidence: 99%