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6CCVD Research

Magnetic relaxometry of methemoglobin by widefield nitrogen-vacancy microscopy

At a Glance

Section titled ā€œAt a Glanceā€
MetadataDetails
Publication Date2024-09-09
JournalApplied Physics Letters
AuthorsSuvechhya Lamichhane, Evelyn Carreto Guevara, Ilja Fescenko, S. H. Liou, Rebecca Y. Lai
InstitutionsUniversity of Latvia, University of Nebraskaā€“Lincoln
Citations2

Abstract

Section titled ā€œAbstractā€

Hemoglobin (Hb) is a multifaceted protein, classified as a metalloprotein, chromoprotein, and globulin. It incorporates iron, which plays a crucial role in transporting oxygen within red blood cells. Hb functions by carrying oxygen from the respiratory organs to diverse tissues in the body, where it releases oxygen to fuel aerobic respiration, thus supporting the organismā€™s metabolic processes. Hb can exist in several forms, primarily distinguished by the oxidation state of the iron in the heme group, including methemoglobin (MetHb). Measuring the concentration of MetHb is crucial because it cannot transport oxygen; hence, higher concentrations of MetHb in the blood causes methemoglobinemia. Here, we use optically detected magnetic relaxometry of paramagnetic iron spins in MetHb drop-cast onto a nanostructured diamond doped with shallow high-density nitrogen-vacancy (NV) spin qubits. We vary the concentration of MetHb in the range of 6 Ɨ 106-1.8 Ɨ 107 adsorbed Fe+3 spins per micrometer squared and observe an increase in the NV relaxation rate Ī“1 (=1/T1, where T1 is the NV spin lattice relaxation time) up to 2 Ɨ 103 sāˆ’1. NV magnetic relaxometry of MetHb in phosphate-buffered saline solution shows a similar effect with an increase in Ī“1 to 6.7 Ɨ 103 sāˆ’1 upon increasing the MetHb concentration to 100 Ī¼M. The increase in NV Ī“1 is explained by the increased spin noise coming from the Fe+3 spins present in MetHb proteins. This study presents an additional usage of NV quantum sensors to detect paramagnetic centers of biomolecules at volumes below 100 picoliter.

Tech Support

Section titled ā€œTech Supportā€

Original Source

Section titled ā€œOriginal Sourceā€

References

Section titled ā€œReferencesā€
  1. 2020 - Hemoglobin: Structure, function and allostery [Crossref]
  2. 1975 - Hemoglobin function, oxygen affinity, and erythropoietin [Crossref]
  3. 1990 - Hemoglobin and hematocrit
  4. 2002 - Structures of human oxy- and deoxyhaemoglobin at different levels of humidity: Variability in the T state [Crossref]
  5. 2010 - Anesthetic experience of methemoglobinemia detected during general anesthesia for gastrectomy of advanced gastric cancerā€”A case report [Crossref]
  6. 2021 - Recommendations for diagnosis and treatment of methemoglobinemia [Crossref]
  7. 2006 - EPR study of the hemoglobin rotational correlation time and microviscosity during the polymerization of hemoglobin S [Crossref]
  8. 1969 - Hemoglobin A: An electron paramagnetic resonance study of the effects of interchain contacts on the heme symmetry of high-spin and low-spin derivatives of ferric alpha chains [Crossref]
  9. 1995 - 1H-NMR investigation of the oxygenation of hemoglobin in intact human red blood cells [Crossref]
  10. 2019 - NMR experiments redefine the hemoglobin binding properties of bacterial NEAr-iron transporter domains [Crossref]

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