P90 Hydrogen sulfide activation by hemeproteins: Implications of the sulfheme scenario

López‐Garriga, Juan; Wymore, Troy; Pietri, Ruth; Román-Morales, Elddie; Ríos-González, Bessie B.; Arbelo, Hector

doi:10.1016/j.niox.2014.03.140

Nitric Oxide

2014

DOI: 10.1016/j.niox.2014.03.140

|View full text |Cite

P90 Hydrogen sulfide activation by hemeproteins: Implications of the sulfheme scenario

Juan López‐Garriga

Troy Wymore

Ruth Pietri

et al.

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...

Citation Types

Supporting

Mentioning

Contrasting

Year Published

2016

2019

Publication Types

Select...

Article2

Relationship

Self Cite0

Independent2

Authors

Journals

Cited by 2 publications

(1 citation statement)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Data suggest that this residue allow that metMb in the presence of H 2 S and hydrogen peroxide produces the incorporation of a sulfur atom in the pyrrole B of the heme-porphyrin generating a species known as sulfMb. This compound has a green color and a characteristic electronic transition at 620 nm[20] [22][45]. To confirm that encapsulates metMb is active toward H 2 S, a similar experiment was performed, where this heme protein was exposed to a 1:5 ratio of H 2 O 2 and H 2 S solutions, respectively.Figure 4inset shows the presence of a band at 617 nm, which can be attributed to the…”

mentioning

confidence: 99%

Transfer and Reactivity of Hydrogen Sulfide with Immobilized Hemeproteins in Polymeric Matrix

Vargas-Santiago¹,

López‐Garriga²

2019

JEAS

View full text Add to dashboard Cite

Hydrogen sulfide (H 2 S) has been related to be toxic and to have a role in human physiological functions. Therefore, there is a necessity to comprehend ways to scavenger hydrogen sulfide from different media. Here, we used recombinant metaquo-Hemoglobin I (metHbI) from Lucina pectinata and metaquo-myoglobin (metMb) encapsulated in the tetramethyl orthosilicate gel (TMOS), to facilitate the understanding of H 2 S transfer toward these metaquo-hemeproteins. In this sol-gel environment, metHbI binds and releases H 2 S with rate constants of 0.0597 M −1 •s −1 and 6.67 × 10 −5 s −1 , respectively. The process generates an H 2 S affinity constant (k on /k off) of 8.9 × 10 2 M −1 , which is 10 7 lowers than the analogous constant in solution (6.3 × 10 9 M −1). Although the H 2 S k off for the rHbI-H 2 S complex is almost similar with both sol-gel and solution. To further understand how the H 2 S k off from rHbI-H 2 S in solution (5 µM) is influenced by the protein concentration gradient, metHbI and metMb (25 µM) encapsulated in TMOS sol-gel. Under these circumstances, the H 2 S transfer from a solution of the rHbI-H 2 S complex to encapsulated hemeprotein resulted in k off values of 1.90 × 10 −4 s −1 , and 2.09 × 10 −4 s −1 leading to the formation of rHbI-H 2 S and Mb-H 2 S species, respectively. The results suggest that the: 1) extreme ionic TMOS construct limits the H 2 S pathways to reach the hemeprotein active center, 2) possible interaction with metHbI hydrophilic forces increases the hydrogen bonding networking and decreases the H 2 S association constant, 3) hemeproteins concentration gradients between solution and sol-gels also influence its hydrogen sulfide transfer. In the presence of oxygen or hydrogen peroxide metMb generated a mixture of Mb-H 2 S and sulfmyoglobin derivative, while encapsulated metHbI reaction did not produce the sulfheme species. Consequently, the results show that metHbI encapsulated in TMOS is an excellent trap for H 2 S from solution or gas media.

show abstract

mentioning

confidence: 99%

Transfer and Reactivity of Hydrogen Sulfide with Immobilized Hemeproteins in Polymeric Matrix

Vargas-Santiago¹,

López‐Garriga²

2019

JEAS

View full text Add to dashboard Cite

show abstract

Oxidative hemoglobin reactions: Applications to drug metabolism

Spolitak

Hollenberg

Ballou

2016

Archives of Biochemistry and Biophysics

View full text Add to dashboard Cite

scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.

Contact Info

hi@scite.ai

10624 S. Eastern Ave., Ste. A-614

Henderson, NV 89052, USA

Blog Terms and Conditions API Terms Privacy Policy Contact Cookie Preferences Do Not Sell or Share My Personal Information

Made with 💙 for researchers

Part of the Research Solutions Family.

P90 Hydrogen sulfide activation by hemeproteins: Implications of the sulfheme scenario

Cited by 2 publications

References 0 publications

Transfer and Reactivity of Hydrogen Sulfide with Immobilized Hemeproteins in Polymeric Matrix

Transfer and Reactivity of Hydrogen Sulfide with Immobilized Hemeproteins in Polymeric Matrix

Oxidative hemoglobin reactions: Applications to drug metabolism

Contact Info

Product

Resources

About